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WW and SH3 domains, two different scaffolds to recognize proline‐rich ligands

Macias, Maria J., Wiesner, Silke, Sudol, Marius·2002·FEBS Letters

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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Crossref · 10.1016/s0014-5793(01)03290-2

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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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CoChat. (2026). Citation check: WW and SH3 domains, two different scaffolds to recognize proline‐rich ligands. https://app.cochat.ai/papers/10.1016/s0014-5793(01)03290-2
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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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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.