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Crystallization of soluble urokinase receptor (suPAR) in complex with urokinase amino-terminal fragment (1–143)
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| Zeitschriftentitel: | Acta Crystallographica Section D Biological Crystallography |
|---|---|
| Personen und Körperschaften: | , , , , , |
| In: | Acta Crystallographica Section D Biological Crystallography, 61, 2005, 6, S. 697-700 |
| Format: | E-Article |
| Sprache: | Unbestimmt |
| veröffentlicht: |
International Union of Crystallography (IUCr)
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| Schlagwörter: |
| author_facet |
Huang, Mingdong Mazar, Andrew P. Parry, Graham Higazi, Abd Al-Roof Kuo, Alice Cines, Douglas B. Huang, Mingdong Mazar, Andrew P. Parry, Graham Higazi, Abd Al-Roof Kuo, Alice Cines, Douglas B. |
|---|---|
| author |
Huang, Mingdong Mazar, Andrew P. Parry, Graham Higazi, Abd Al-Roof Kuo, Alice Cines, Douglas B. |
| spellingShingle |
Huang, Mingdong Mazar, Andrew P. Parry, Graham Higazi, Abd Al-Roof Kuo, Alice Cines, Douglas B. Acta Crystallographica Section D Biological Crystallography Crystallization of soluble urokinase receptor (suPAR) in complex with urokinase amino-terminal fragment (1–143) General Medicine Structural Biology |
| author_sort |
huang, mingdong |
| spelling |
Huang, Mingdong Mazar, Andrew P. Parry, Graham Higazi, Abd Al-Roof Kuo, Alice Cines, Douglas B. 0907-4449 International Union of Crystallography (IUCr) General Medicine Structural Biology http://dx.doi.org/10.1107/s0907444905014174 <jats:p>Urokinase-type plasminogen activator (urokinase, uPA) and its receptor, uPAR, have been implicated in cell adhesion, migration, tissue remodelling and tumour-cell invasion. uPAR has three domains and is anchored to membranes by a glycosyl-phosphatidylinositol (GPI) anchor. Recombinant uPAR without its GPI anchor, soluble uPAR (suPAR), tends to oligomerize, making it difficult to crystallize. The amino-terminal fragment (ATF) of uPA is the major receptor-binding determinant in suPAR and binds to suPAR with nanomolar affinity, indistinguishable from membrane-bound uPAR. It is shown that uPA is capable of dissociating the oligomerization of suPAR and the crystallization of the suPAR–ATF complex is reported here. The resulting crystals diffract to 3.1 Å using a synchrotron X-ray source.</jats:p> Crystallization of soluble urokinase receptor (suPAR) in complex with urokinase amino-terminal fragment (1–143) Acta Crystallographica Section D Biological Crystallography |
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| title |
Crystallization of soluble urokinase receptor (suPAR) in complex with urokinase amino-terminal fragment (1–143) |
| title_unstemmed |
Crystallization of soluble urokinase receptor (suPAR) in complex with urokinase amino-terminal fragment (1–143) |
| title_full |
Crystallization of soluble urokinase receptor (suPAR) in complex with urokinase amino-terminal fragment (1–143) |
| title_fullStr |
Crystallization of soluble urokinase receptor (suPAR) in complex with urokinase amino-terminal fragment (1–143) |
| title_full_unstemmed |
Crystallization of soluble urokinase receptor (suPAR) in complex with urokinase amino-terminal fragment (1–143) |
| title_short |
Crystallization of soluble urokinase receptor (suPAR) in complex with urokinase amino-terminal fragment (1–143) |
| title_sort |
crystallization of soluble urokinase receptor (supar) in complex with urokinase amino-terminal fragment (1–143) |
| topic |
General Medicine Structural Biology |
| url |
http://dx.doi.org/10.1107/s0907444905014174 |
| publishDate |
2005 |
| physical |
697-700 |
| description |
<jats:p>Urokinase-type plasminogen activator (urokinase, uPA) and its receptor, uPAR, have been implicated in cell adhesion, migration, tissue remodelling and tumour-cell invasion. uPAR has three domains and is anchored to membranes by a glycosyl-phosphatidylinositol (GPI) anchor. Recombinant uPAR without its GPI anchor, soluble uPAR (suPAR), tends to oligomerize, making it difficult to crystallize. The amino-terminal fragment (ATF) of uPA is the major receptor-binding determinant in suPAR and binds to suPAR with nanomolar affinity, indistinguishable from membrane-bound uPAR. It is shown that uPA is capable of dissociating the oligomerization of suPAR and the crystallization of the suPAR–ATF complex is reported here. The resulting crystals diffract to 3.1 Å using a synchrotron X-ray source.</jats:p> |
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| author | Huang, Mingdong, Mazar, Andrew P., Parry, Graham, Higazi, Abd Al-Roof, Kuo, Alice, Cines, Douglas B. |
| author_facet | Huang, Mingdong, Mazar, Andrew P., Parry, Graham, Higazi, Abd Al-Roof, Kuo, Alice, Cines, Douglas B., Huang, Mingdong, Mazar, Andrew P., Parry, Graham, Higazi, Abd Al-Roof, Kuo, Alice, Cines, Douglas B. |
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| description | <jats:p>Urokinase-type plasminogen activator (urokinase, uPA) and its receptor, uPAR, have been implicated in cell adhesion, migration, tissue remodelling and tumour-cell invasion. uPAR has three domains and is anchored to membranes by a glycosyl-phosphatidylinositol (GPI) anchor. Recombinant uPAR without its GPI anchor, soluble uPAR (suPAR), tends to oligomerize, making it difficult to crystallize. The amino-terminal fragment (ATF) of uPA is the major receptor-binding determinant in suPAR and binds to suPAR with nanomolar affinity, indistinguishable from membrane-bound uPAR. It is shown that uPA is capable of dissociating the oligomerization of suPAR and the crystallization of the suPAR–ATF complex is reported here. The resulting crystals diffract to 3.1 Å using a synchrotron X-ray source.</jats:p> |
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| spelling | Huang, Mingdong Mazar, Andrew P. Parry, Graham Higazi, Abd Al-Roof Kuo, Alice Cines, Douglas B. 0907-4449 International Union of Crystallography (IUCr) General Medicine Structural Biology http://dx.doi.org/10.1107/s0907444905014174 <jats:p>Urokinase-type plasminogen activator (urokinase, uPA) and its receptor, uPAR, have been implicated in cell adhesion, migration, tissue remodelling and tumour-cell invasion. uPAR has three domains and is anchored to membranes by a glycosyl-phosphatidylinositol (GPI) anchor. Recombinant uPAR without its GPI anchor, soluble uPAR (suPAR), tends to oligomerize, making it difficult to crystallize. The amino-terminal fragment (ATF) of uPA is the major receptor-binding determinant in suPAR and binds to suPAR with nanomolar affinity, indistinguishable from membrane-bound uPAR. It is shown that uPA is capable of dissociating the oligomerization of suPAR and the crystallization of the suPAR–ATF complex is reported here. The resulting crystals diffract to 3.1 Å using a synchrotron X-ray source.</jats:p> Crystallization of soluble urokinase receptor (suPAR) in complex with urokinase amino-terminal fragment (1–143) Acta Crystallographica Section D Biological Crystallography |
| spellingShingle | Huang, Mingdong, Mazar, Andrew P., Parry, Graham, Higazi, Abd Al-Roof, Kuo, Alice, Cines, Douglas B., Acta Crystallographica Section D Biological Crystallography, Crystallization of soluble urokinase receptor (suPAR) in complex with urokinase amino-terminal fragment (1–143), General Medicine, Structural Biology |
| title | Crystallization of soluble urokinase receptor (suPAR) in complex with urokinase amino-terminal fragment (1–143) |
| title_full | Crystallization of soluble urokinase receptor (suPAR) in complex with urokinase amino-terminal fragment (1–143) |
| title_fullStr | Crystallization of soluble urokinase receptor (suPAR) in complex with urokinase amino-terminal fragment (1–143) |
| title_full_unstemmed | Crystallization of soluble urokinase receptor (suPAR) in complex with urokinase amino-terminal fragment (1–143) |
| title_short | Crystallization of soluble urokinase receptor (suPAR) in complex with urokinase amino-terminal fragment (1–143) |
| title_sort | crystallization of soluble urokinase receptor (supar) in complex with urokinase amino-terminal fragment (1–143) |
| title_unstemmed | Crystallization of soluble urokinase receptor (suPAR) in complex with urokinase amino-terminal fragment (1–143) |
| topic | General Medicine, Structural Biology |
| url | http://dx.doi.org/10.1107/s0907444905014174 |