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WW and SH3 domains, two different scaffolds to recognize proline‐rich ligands
Abstract
WW domains are small protein modules composed of approximately 40 amino acids. These domains fold as a stable, triple stranded β‐sheet and recognize proline‐containing ligands. WW domains are found in many different signaling and structural proteins, often localized in the cytoplasm as well as in the cell nucleus. Based on analyses of seven structures of WW domains, we discuss their diverse binding preferences and sequence conservation patterns. While modeling WW domains for which structures have not been determined we uncovered a case of potential molecular and functional convergence between WW and SH3 domains. The binding surface of the modeled WW domain of Npw38 protein shows a remarkable similarity to the SH3 domain of Sem5 protein, confirming biochemical data on similar binding predilections of both domains.
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Citations
Cites
Modular binding domains in signal transduction proteins
Cohen, G. B., Ren, R., & Baltimore, D. (1995) · Cell · doi:10.1016/0092-8674(95)90406-9 · Cited by 951
The WW domain: a signalling site in dystrophin?
Bork, P., & Sudol, M. (1994) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(94)90053-1 · Cited by 388
Self-citation
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Metadata
- Authors
- Macias, M. J., Wiesner, S., & Sudol, M.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2001-12-20
- Volume
- 513
- Issue
- 1
- Pages
- 30-37
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2043186621
- Cited by
- 478
- References
- 2
- FWCI
- 7.17
- Type
- journal article
- Language
- en
- Open access
- closed
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- Macias, M. J., Wiesner, S., & Sudol, M. (2002). WW and SH3 domains, two different scaffolds to recognize proline‐rich ligands. FEBS Letters. https://doi.org/10.1016/s0014-5793(01)03290-2
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