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Elucidation of the binding preferences of peptide recognition modules: SH3 and PDZ domains
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| Zeitschriftentitel: | FEBS Letters |
|---|---|
| Personen und Körperschaften: | , , |
| In: | FEBS Letters, 586, 2012, 17, S. 2631-2637 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
|
| Schlagwörter: |
| author_facet |
Teyra, Joan Sidhu, Sachdev S. Kim, Philip M. Teyra, Joan Sidhu, Sachdev S. Kim, Philip M. |
|---|---|
| author |
Teyra, Joan Sidhu, Sachdev S. Kim, Philip M. |
| spellingShingle |
Teyra, Joan Sidhu, Sachdev S. Kim, Philip M. FEBS Letters Elucidation of the binding preferences of peptide recognition modules: SH3 and PDZ domains Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics |
| author_sort |
teyra, joan |
| spelling |
Teyra, Joan Sidhu, Sachdev S. Kim, Philip M. 0014-5793 1873-3468 Wiley Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1016/j.febslet.2012.05.043 <jats:p>Peptide‐binding domains play a critical role in regulation of cellular processes by mediating protein interactions involved in signalling. In recent years, the development of large‐scale technologies has enabled exhaustive studies on the peptide recognition preferences for a number of peptide‐binding domain families. These efforts have provided significant insights into the binding specificities of these modular domains. Many research groups have taken advantage of this unprecedented volume of specificity data and have developed a variety of new algorithms for the prediction of binding specificities of peptide‐binding domains and for the prediction of their natural binding targets. This knowledge has also been applied to the design of synthetic peptide‐binding domains in order to rewire protein–protein interaction networks. Here, we describe how these experimental technologies have impacted on our understanding of peptide‐binding domain specificities and on the elucidation of their natural ligands. We discuss SH3 and PDZ domains as well characterized examples, and we explore the feasibility of expanding high‐throughput experiments to other peptide‐binding domains.</jats:p> Elucidation of the binding preferences of peptide recognition modules: SH3 and PDZ domains FEBS Letters |
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10.1016/j.febslet.2012.05.043 |
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Wiley, 2012 |
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Wiley, 2012 |
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| title |
Elucidation of the binding preferences of peptide recognition modules: SH3 and PDZ domains |
| title_unstemmed |
Elucidation of the binding preferences of peptide recognition modules: SH3 and PDZ domains |
| title_full |
Elucidation of the binding preferences of peptide recognition modules: SH3 and PDZ domains |
| title_fullStr |
Elucidation of the binding preferences of peptide recognition modules: SH3 and PDZ domains |
| title_full_unstemmed |
Elucidation of the binding preferences of peptide recognition modules: SH3 and PDZ domains |
| title_short |
Elucidation of the binding preferences of peptide recognition modules: SH3 and PDZ domains |
| title_sort |
elucidation of the binding preferences of peptide recognition modules: sh3 and pdz domains |
| topic |
Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics |
| url |
http://dx.doi.org/10.1016/j.febslet.2012.05.043 |
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2012 |
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2631-2637 |
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<jats:p>Peptide‐binding domains play a critical role in regulation of cellular processes by mediating protein interactions involved in signalling. In recent years, the development of large‐scale technologies has enabled exhaustive studies on the peptide recognition preferences for a number of peptide‐binding domain families. These efforts have provided significant insights into the binding specificities of these modular domains. Many research groups have taken advantage of this unprecedented volume of specificity data and have developed a variety of new algorithms for the prediction of binding specificities of peptide‐binding domains and for the prediction of their natural binding targets. This knowledge has also been applied to the design of synthetic peptide‐binding domains in order to rewire protein–protein interaction networks. Here, we describe how these experimental technologies have impacted on our understanding of peptide‐binding domain specificities and on the elucidation of their natural ligands. We discuss SH3 and PDZ domains as well characterized examples, and we explore the feasibility of expanding high‐throughput experiments to other peptide‐binding domains.</jats:p> |
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| description | <jats:p>Peptide‐binding domains play a critical role in regulation of cellular processes by mediating protein interactions involved in signalling. In recent years, the development of large‐scale technologies has enabled exhaustive studies on the peptide recognition preferences for a number of peptide‐binding domain families. These efforts have provided significant insights into the binding specificities of these modular domains. Many research groups have taken advantage of this unprecedented volume of specificity data and have developed a variety of new algorithms for the prediction of binding specificities of peptide‐binding domains and for the prediction of their natural binding targets. This knowledge has also been applied to the design of synthetic peptide‐binding domains in order to rewire protein–protein interaction networks. Here, we describe how these experimental technologies have impacted on our understanding of peptide‐binding domain specificities and on the elucidation of their natural ligands. We discuss SH3 and PDZ domains as well characterized examples, and we explore the feasibility of expanding high‐throughput experiments to other peptide‐binding domains.</jats:p> |
| doi_str_mv | 10.1016/j.febslet.2012.05.043 |
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| series | FEBS Letters |
| source_id | 49 |
| spelling | Teyra, Joan Sidhu, Sachdev S. Kim, Philip M. 0014-5793 1873-3468 Wiley Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1016/j.febslet.2012.05.043 <jats:p>Peptide‐binding domains play a critical role in regulation of cellular processes by mediating protein interactions involved in signalling. In recent years, the development of large‐scale technologies has enabled exhaustive studies on the peptide recognition preferences for a number of peptide‐binding domain families. These efforts have provided significant insights into the binding specificities of these modular domains. Many research groups have taken advantage of this unprecedented volume of specificity data and have developed a variety of new algorithms for the prediction of binding specificities of peptide‐binding domains and for the prediction of their natural binding targets. This knowledge has also been applied to the design of synthetic peptide‐binding domains in order to rewire protein–protein interaction networks. Here, we describe how these experimental technologies have impacted on our understanding of peptide‐binding domain specificities and on the elucidation of their natural ligands. We discuss SH3 and PDZ domains as well characterized examples, and we explore the feasibility of expanding high‐throughput experiments to other peptide‐binding domains.</jats:p> Elucidation of the binding preferences of peptide recognition modules: SH3 and PDZ domains FEBS Letters |
| spellingShingle | Teyra, Joan, Sidhu, Sachdev S., Kim, Philip M., FEBS Letters, Elucidation of the binding preferences of peptide recognition modules: SH3 and PDZ domains, Cell Biology, Genetics, Molecular Biology, Biochemistry, Structural Biology, Biophysics |
| title | Elucidation of the binding preferences of peptide recognition modules: SH3 and PDZ domains |
| title_full | Elucidation of the binding preferences of peptide recognition modules: SH3 and PDZ domains |
| title_fullStr | Elucidation of the binding preferences of peptide recognition modules: SH3 and PDZ domains |
| title_full_unstemmed | Elucidation of the binding preferences of peptide recognition modules: SH3 and PDZ domains |
| title_short | Elucidation of the binding preferences of peptide recognition modules: SH3 and PDZ domains |
| title_sort | elucidation of the binding preferences of peptide recognition modules: sh3 and pdz domains |
| title_unstemmed | Elucidation of the binding preferences of peptide recognition modules: SH3 and PDZ domains |
| topic | Cell Biology, Genetics, Molecular Biology, Biochemistry, Structural Biology, Biophysics |
| url | http://dx.doi.org/10.1016/j.febslet.2012.05.043 |