4LN2

The second SH3 domain from CAP/Ponsin in complex with proline rich peptide from Vinculin

4LN2 の概要

• エントリーDOI: 10.2210/pdb4ln2/pdb
• 関連するPDBエントリー: 2MOX 4LNP
• 分子名称: Sorbin and SH3 domain-containing protein 1, proline rich peptide (3 entities in total)
• 機能のキーワード: sh3 domain, cell migration, focal adhesion, signaling protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cell junction, adherens junction: Q9BX66; Cytoplasm, cytoskeleton : P18206
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 9158.45

構造登録者

Zhao, D.,Li, F.,Wu, J.,Shi, Y.,Zhang, Z.,Gong, Q. (登録日: 2013-07-11, 公開日: 2014-05-28, 最終更新日: 2023-11-08)

主引用文献

Zhao, D.,Wang, X.,Peng, J.,Wang, C.,Li, F.,Sun, Q.,Zhang, Y.,Zhang, J.,Cai, G.,Zuo, X.,Wu, J.,Shi, Y.,Zhang, Z.,Gong, Q.
Structural investigation of the interaction between the tandem SH3 domains of c-Cbl-associated protein and vinculin
J.Struct.Biol., 187:194-205, 2014

PubMed Abstract: c-Cbl-associated protein (CAP) is an important cytoskeletal adaptor protein involved in the regulation of adhesion turnover. The interaction between CAP and vinculin is critical for the recruitment of CAP to focal adhesions. The tandem SH3 domains (herein termed SH3a and SH3b) of CAP are responsible for its interaction with vinculin. However, the structural mechanism underlying the interaction between CAP and vinculin is poorly understood. In this manuscript, we report the solution structure of the tandem SH3 domains of CAP. Our NMR and ITC data indicate that the SH3a and SH3b domains of CAP simultaneously bind to a long proline-rich region of vinculin with different binding specificities. Furthermore, the crystal structures of the individual SH3a and SH3b domains complexed with their substrate peptides indicate that Q807(SH3a) and D881(SH3b) are the critical residues determining the different binding specificities of the SH3 domains. Based on the obtained structural information, a model of the SH3ab-vinculin complex was generated using MD simulation and SAXS data.

PubMed: 24878663
DOI: 10.1016/j.jsb.2014.05.009

実験手法

X-RAY DIFFRACTION (1 Å)