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Tetramerization of human guanylate‐binding protein 1 is mediated by coiled‐coil formation of the C‐terminal α‐helices
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| Zeitschriftentitel: | The FEBS Journal |
|---|---|
| Personen und Körperschaften: | , , , , , , , |
| In: | The FEBS Journal, 279, 2012, 14, S. 2544-2554 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
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| Schlagwörter: |
| author_facet |
Syguda, Adrian Bauer, Michael Benscheid, Utz Ostler, Nicole Naschberger, Elisabeth Ince, Semra Stürzl, Michael Herrmann, Christian Syguda, Adrian Bauer, Michael Benscheid, Utz Ostler, Nicole Naschberger, Elisabeth Ince, Semra Stürzl, Michael Herrmann, Christian |
|---|---|
| author |
Syguda, Adrian Bauer, Michael Benscheid, Utz Ostler, Nicole Naschberger, Elisabeth Ince, Semra Stürzl, Michael Herrmann, Christian |
| spellingShingle |
Syguda, Adrian Bauer, Michael Benscheid, Utz Ostler, Nicole Naschberger, Elisabeth Ince, Semra Stürzl, Michael Herrmann, Christian The FEBS Journal Tetramerization of human guanylate‐binding protein 1 is mediated by coiled‐coil formation of the C‐terminal α‐helices Cell Biology Molecular Biology Biochemistry |
| author_sort |
syguda, adrian |
| spelling |
Syguda, Adrian Bauer, Michael Benscheid, Utz Ostler, Nicole Naschberger, Elisabeth Ince, Semra Stürzl, Michael Herrmann, Christian 1742-464X 1742-4658 Wiley Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1111/j.1742-4658.2012.08637.x <jats:p>The human guanylate‐binding protein 1 (hGBP1) is a large GTP‐binding protein belonging to the dynamin family, a common feature of which is nucleotide‐dependent assembly to homotypic oligomers. Assembly leads to stimulation of GTPase activity, which, in the case of dynamin, is responsible for scission of vesicles from membranes. By yeast two‐hybrid and biochemical experiments we addressed intermolecular interactions between all subdomains of hGBP1 and identified the C‐terminal subdomain, α12/13, as a new interaction site for self‐assembly. α12/13 represents a stable subdomain of hGBP1, as shown by CD spectroscopy. In addition to contacts between GTPase domains leading to dimer formation, the interaction between two α12/13 subdomains, in the course of GTP hydrolysis, results in tetramer formation of the protein. With the help of CD spectroscopy we showed coiled‐coil formation of two α12/13 subdomains and concentration‐dependent measurements allow estimating a value for the dissociation constant of 7.3 μ<jats:sc>m</jats:sc>. We suggest GTP hydrolysis‐driven release of the α12/13 subdomain, making it available for coiled‐coil formation. Furthermore, we can demonstrate the biological relevance of hGBP1 tetramer formation in living cells by chemical cross‐link experiments.</jats:p><jats:p><jats:bold>Structured digital abstract</jats:bold></jats:p><jats:p><jats:list list-type="explicit-label"> <jats:list-item><jats:p> <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.uniprot.org/uniprot/P32455">hGBP1</jats:ext-link> and <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.uniprot.org/uniprot/P32455">hGBP1</jats:ext-link> <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0407">bind</jats:ext-link> by <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0030">cross‐linking study</jats:ext-link> (<jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://mint.bio.uniroma2.it/mint/search/interaction.do?interactionAc=MINT-8375154">View interaction</jats:ext-link>)</jats:p></jats:list-item> <jats:list-item><jats:p> <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.uniprot.org/uniprot/P32455">hGBP1</jats:ext-link> and <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.uniprot.org/uniprot/P32455">hGBP1</jats:ext-link> <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0407">bind</jats:ext-link> by <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0071">molecular sieving</jats:ext-link> (View Interaction: <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://mint.bio.uniroma2.it/mint/search/interaction.do?interactionAc=MINT-8375190">1</jats:ext-link>, <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://mint.bio.uniroma2.it/mint/search/interaction.do?interactionAc=MINT-8375198">2</jats:ext-link>)</jats:p></jats:list-item> <jats:list-item><jats:p> <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.uniprot.org/uniprot/P32455">hGBP1</jats:ext-link> <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0915">physically interacts</jats:ext-link> with <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.uniprot.org/uniprot/P32455">hGBP1</jats:ext-link> by <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0018">two hybrid</jats:ext-link> (View Interaction: <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://mint.bio.uniroma2.it/mint/search/interaction.do?interactionAc=MINT-8375104">1</jats:ext-link>, <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://mint.bio.uniroma2.it/mint/search/interaction.do?interactionAc=MINT-8375120">2</jats:ext-link>, <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://mint.bio.uniroma2.it/mint/search/interaction.do?interactionAc=MINT-8375135">3</jats:ext-link>)</jats:p></jats:list-item> </jats:list></jats:p> Tetramerization of human guanylate‐binding protein 1 is mediated by coiled‐coil formation of the C‐terminal α‐helices The FEBS Journal |
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Wiley, 2012 |
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1742-464X 1742-4658 |
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syguda2012tetramerizationofhumanguanylatebindingprotein1ismediatedbycoiledcoilformationofthecterminalahelices |
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2012 |
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| title |
Tetramerization of human guanylate‐binding protein 1 is mediated by coiled‐coil formation of the C‐terminal α‐helices |
| title_unstemmed |
Tetramerization of human guanylate‐binding protein 1 is mediated by coiled‐coil formation of the C‐terminal α‐helices |
| title_full |
Tetramerization of human guanylate‐binding protein 1 is mediated by coiled‐coil formation of the C‐terminal α‐helices |
| title_fullStr |
Tetramerization of human guanylate‐binding protein 1 is mediated by coiled‐coil formation of the C‐terminal α‐helices |
| title_full_unstemmed |
Tetramerization of human guanylate‐binding protein 1 is mediated by coiled‐coil formation of the C‐terminal α‐helices |
| title_short |
Tetramerization of human guanylate‐binding protein 1 is mediated by coiled‐coil formation of the C‐terminal α‐helices |
| title_sort |
tetramerization of human guanylate‐binding protein 1 is mediated by coiled‐coil formation of the c‐terminal α‐helices |
| topic |
Cell Biology Molecular Biology Biochemistry |
| url |
http://dx.doi.org/10.1111/j.1742-4658.2012.08637.x |
| publishDate |
2012 |
| physical |
2544-2554 |
| description |
<jats:p>The human guanylate‐binding protein 1 (hGBP1) is a large GTP‐binding protein belonging to the dynamin family, a common feature of which is nucleotide‐dependent assembly to homotypic oligomers. Assembly leads to stimulation of GTPase activity, which, in the case of dynamin, is responsible for scission of vesicles from membranes. By yeast two‐hybrid and biochemical experiments we addressed intermolecular interactions between all subdomains of hGBP1 and identified the C‐terminal subdomain, α12/13, as a new interaction site for self‐assembly. α12/13 represents a stable subdomain of hGBP1, as shown by CD spectroscopy. In addition to contacts between GTPase domains leading to dimer formation, the interaction between two α12/13 subdomains, in the course of GTP hydrolysis, results in tetramer formation of the protein. With the help of CD spectroscopy we showed coiled‐coil formation of two α12/13 subdomains and concentration‐dependent measurements allow estimating a value for the dissociation constant of 7.3 μ<jats:sc>m</jats:sc>. We suggest GTP hydrolysis‐driven release of the α12/13 subdomain, making it available for coiled‐coil formation. Furthermore, we can demonstrate the biological relevance of hGBP1 tetramer formation in living cells by chemical cross‐link experiments.</jats:p><jats:p><jats:bold>Structured digital abstract</jats:bold></jats:p><jats:p><jats:list list-type="explicit-label">
<jats:list-item><jats:p> <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.uniprot.org/uniprot/P32455">hGBP1</jats:ext-link> and <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.uniprot.org/uniprot/P32455">hGBP1</jats:ext-link> <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0407">bind</jats:ext-link> by <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0030">cross‐linking study</jats:ext-link> (<jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://mint.bio.uniroma2.it/mint/search/interaction.do?interactionAc=MINT-8375154">View interaction</jats:ext-link>)</jats:p></jats:list-item>
<jats:list-item><jats:p> <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.uniprot.org/uniprot/P32455">hGBP1</jats:ext-link> and <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.uniprot.org/uniprot/P32455">hGBP1</jats:ext-link> <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0407">bind</jats:ext-link> by <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0071">molecular sieving</jats:ext-link> (View Interaction: <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://mint.bio.uniroma2.it/mint/search/interaction.do?interactionAc=MINT-8375190">1</jats:ext-link>, <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://mint.bio.uniroma2.it/mint/search/interaction.do?interactionAc=MINT-8375198">2</jats:ext-link>)</jats:p></jats:list-item>
<jats:list-item><jats:p> <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.uniprot.org/uniprot/P32455">hGBP1</jats:ext-link> <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0915">physically interacts</jats:ext-link> with <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.uniprot.org/uniprot/P32455">hGBP1</jats:ext-link> by <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0018">two hybrid</jats:ext-link> (View Interaction: <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://mint.bio.uniroma2.it/mint/search/interaction.do?interactionAc=MINT-8375104">1</jats:ext-link>, <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://mint.bio.uniroma2.it/mint/search/interaction.do?interactionAc=MINT-8375120">2</jats:ext-link>, <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://mint.bio.uniroma2.it/mint/search/interaction.do?interactionAc=MINT-8375135">3</jats:ext-link>)</jats:p></jats:list-item>
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| description | <jats:p>The human guanylate‐binding protein 1 (hGBP1) is a large GTP‐binding protein belonging to the dynamin family, a common feature of which is nucleotide‐dependent assembly to homotypic oligomers. Assembly leads to stimulation of GTPase activity, which, in the case of dynamin, is responsible for scission of vesicles from membranes. By yeast two‐hybrid and biochemical experiments we addressed intermolecular interactions between all subdomains of hGBP1 and identified the C‐terminal subdomain, α12/13, as a new interaction site for self‐assembly. α12/13 represents a stable subdomain of hGBP1, as shown by CD spectroscopy. In addition to contacts between GTPase domains leading to dimer formation, the interaction between two α12/13 subdomains, in the course of GTP hydrolysis, results in tetramer formation of the protein. With the help of CD spectroscopy we showed coiled‐coil formation of two α12/13 subdomains and concentration‐dependent measurements allow estimating a value for the dissociation constant of 7.3 μ<jats:sc>m</jats:sc>. We suggest GTP hydrolysis‐driven release of the α12/13 subdomain, making it available for coiled‐coil formation. Furthermore, we can demonstrate the biological relevance of hGBP1 tetramer formation in living cells by chemical cross‐link experiments.</jats:p><jats:p><jats:bold>Structured digital abstract</jats:bold></jats:p><jats:p><jats:list list-type="explicit-label"> <jats:list-item><jats:p> <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.uniprot.org/uniprot/P32455">hGBP1</jats:ext-link> and <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.uniprot.org/uniprot/P32455">hGBP1</jats:ext-link> <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0407">bind</jats:ext-link> by <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0030">cross‐linking study</jats:ext-link> (<jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://mint.bio.uniroma2.it/mint/search/interaction.do?interactionAc=MINT-8375154">View interaction</jats:ext-link>)</jats:p></jats:list-item> <jats:list-item><jats:p> <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.uniprot.org/uniprot/P32455">hGBP1</jats:ext-link> and <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.uniprot.org/uniprot/P32455">hGBP1</jats:ext-link> <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0407">bind</jats:ext-link> by <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0071">molecular sieving</jats:ext-link> (View Interaction: <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://mint.bio.uniroma2.it/mint/search/interaction.do?interactionAc=MINT-8375190">1</jats:ext-link>, <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://mint.bio.uniroma2.it/mint/search/interaction.do?interactionAc=MINT-8375198">2</jats:ext-link>)</jats:p></jats:list-item> <jats:list-item><jats:p> <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.uniprot.org/uniprot/P32455">hGBP1</jats:ext-link> <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0915">physically interacts</jats:ext-link> with <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.uniprot.org/uniprot/P32455">hGBP1</jats:ext-link> by <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0018">two hybrid</jats:ext-link> (View Interaction: <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://mint.bio.uniroma2.it/mint/search/interaction.do?interactionAc=MINT-8375104">1</jats:ext-link>, <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://mint.bio.uniroma2.it/mint/search/interaction.do?interactionAc=MINT-8375120">2</jats:ext-link>, <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://mint.bio.uniroma2.it/mint/search/interaction.do?interactionAc=MINT-8375135">3</jats:ext-link>)</jats:p></jats:list-item> </jats:list></jats:p> |
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| series | The FEBS Journal |
| source_id | 49 |
| spelling | Syguda, Adrian Bauer, Michael Benscheid, Utz Ostler, Nicole Naschberger, Elisabeth Ince, Semra Stürzl, Michael Herrmann, Christian 1742-464X 1742-4658 Wiley Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1111/j.1742-4658.2012.08637.x <jats:p>The human guanylate‐binding protein 1 (hGBP1) is a large GTP‐binding protein belonging to the dynamin family, a common feature of which is nucleotide‐dependent assembly to homotypic oligomers. Assembly leads to stimulation of GTPase activity, which, in the case of dynamin, is responsible for scission of vesicles from membranes. By yeast two‐hybrid and biochemical experiments we addressed intermolecular interactions between all subdomains of hGBP1 and identified the C‐terminal subdomain, α12/13, as a new interaction site for self‐assembly. α12/13 represents a stable subdomain of hGBP1, as shown by CD spectroscopy. In addition to contacts between GTPase domains leading to dimer formation, the interaction between two α12/13 subdomains, in the course of GTP hydrolysis, results in tetramer formation of the protein. With the help of CD spectroscopy we showed coiled‐coil formation of two α12/13 subdomains and concentration‐dependent measurements allow estimating a value for the dissociation constant of 7.3 μ<jats:sc>m</jats:sc>. We suggest GTP hydrolysis‐driven release of the α12/13 subdomain, making it available for coiled‐coil formation. Furthermore, we can demonstrate the biological relevance of hGBP1 tetramer formation in living cells by chemical cross‐link experiments.</jats:p><jats:p><jats:bold>Structured digital abstract</jats:bold></jats:p><jats:p><jats:list list-type="explicit-label"> <jats:list-item><jats:p> <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.uniprot.org/uniprot/P32455">hGBP1</jats:ext-link> and <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.uniprot.org/uniprot/P32455">hGBP1</jats:ext-link> <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0407">bind</jats:ext-link> by <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0030">cross‐linking study</jats:ext-link> (<jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://mint.bio.uniroma2.it/mint/search/interaction.do?interactionAc=MINT-8375154">View interaction</jats:ext-link>)</jats:p></jats:list-item> <jats:list-item><jats:p> <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.uniprot.org/uniprot/P32455">hGBP1</jats:ext-link> and <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.uniprot.org/uniprot/P32455">hGBP1</jats:ext-link> <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0407">bind</jats:ext-link> by <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0071">molecular sieving</jats:ext-link> (View Interaction: <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://mint.bio.uniroma2.it/mint/search/interaction.do?interactionAc=MINT-8375190">1</jats:ext-link>, <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://mint.bio.uniroma2.it/mint/search/interaction.do?interactionAc=MINT-8375198">2</jats:ext-link>)</jats:p></jats:list-item> <jats:list-item><jats:p> <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.uniprot.org/uniprot/P32455">hGBP1</jats:ext-link> <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0915">physically interacts</jats:ext-link> with <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.uniprot.org/uniprot/P32455">hGBP1</jats:ext-link> by <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0018">two hybrid</jats:ext-link> (View Interaction: <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://mint.bio.uniroma2.it/mint/search/interaction.do?interactionAc=MINT-8375104">1</jats:ext-link>, <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://mint.bio.uniroma2.it/mint/search/interaction.do?interactionAc=MINT-8375120">2</jats:ext-link>, <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="http://mint.bio.uniroma2.it/mint/search/interaction.do?interactionAc=MINT-8375135">3</jats:ext-link>)</jats:p></jats:list-item> </jats:list></jats:p> Tetramerization of human guanylate‐binding protein 1 is mediated by coiled‐coil formation of the C‐terminal α‐helices The FEBS Journal |
| spellingShingle | Syguda, Adrian, Bauer, Michael, Benscheid, Utz, Ostler, Nicole, Naschberger, Elisabeth, Ince, Semra, Stürzl, Michael, Herrmann, Christian, The FEBS Journal, Tetramerization of human guanylate‐binding protein 1 is mediated by coiled‐coil formation of the C‐terminal α‐helices, Cell Biology, Molecular Biology, Biochemistry |
| title | Tetramerization of human guanylate‐binding protein 1 is mediated by coiled‐coil formation of the C‐terminal α‐helices |
| title_full | Tetramerization of human guanylate‐binding protein 1 is mediated by coiled‐coil formation of the C‐terminal α‐helices |
| title_fullStr | Tetramerization of human guanylate‐binding protein 1 is mediated by coiled‐coil formation of the C‐terminal α‐helices |
| title_full_unstemmed | Tetramerization of human guanylate‐binding protein 1 is mediated by coiled‐coil formation of the C‐terminal α‐helices |
| title_short | Tetramerization of human guanylate‐binding protein 1 is mediated by coiled‐coil formation of the C‐terminal α‐helices |
| title_sort | tetramerization of human guanylate‐binding protein 1 is mediated by coiled‐coil formation of the c‐terminal α‐helices |
| title_unstemmed | Tetramerization of human guanylate‐binding protein 1 is mediated by coiled‐coil formation of the C‐terminal α‐helices |
| topic | Cell Biology, Molecular Biology, Biochemistry |
| url | http://dx.doi.org/10.1111/j.1742-4658.2012.08637.x |