3T6G

Structure of the complex between NSP3 (SHEP1) and p130Cas

3T6G の概要

• エントリーDOI: 10.2210/pdb3t6g/pdb
• 関連するPDBエントリー: 3T6A
• 分子名称: SH2 domain-containing protein 3C, Breast cancer anti-estrogen resistance protein 1, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: cdc25-homology domain, gtpase exchange factor, focal-adhesion targeting domain, signaling protein, cell adhesion
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm (By similarity): Q8N5H7; Cell junction, focal adhesion: P56945
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 125155.88

構造登録者

Mace, P.D.,Robinson, H.,Riedl, S.J. (登録日: 2011-07-28, 公開日: 2011-11-23, 最終更新日: 2024-02-28)

主引用文献

Mace, P.D.,Wallez, Y.,Dobaczewska, M.K.,Lee, J.J.,Robinson, H.,Pasquale, E.B.,Riedl, S.J.
NSP-Cas protein structures reveal a promiscuous interaction module in cell signaling.
Nat.Struct.Mol.Biol., 18:1381-1387, 2011

PubMed Abstract: Members of the novel SH2-containing protein (NSP) and Crk-associated substrate (Cas) protein families form multidomain signaling platforms that mediate cell migration and invasion through a collection of distinct signaling motifs. Members of each family interact via their respective C-terminal domains, but the mechanism of this association has remained enigmatic. Here we present the crystal structures of the C-terminal domain from the NSP protein BCAR3 and the complex of NSP3 with p130Cas. BCAR3 adopts the Cdc25-homology fold of Ras GTPase exchange factors, but it has a 'closed' conformation incapable of enzymatic activity. The structure of the NSP3-p130Cas complex reveals that this closed conformation is instrumental for interaction of NSP proteins with a focal adhesion-targeting domain present in Cas proteins. This enzyme-to-adaptor conversion enables high-affinity, yet promiscuous, interactions between NSP and Cas proteins and represents an unprecedented mechanistic paradigm linking cellular signaling networks.

PubMed: 22081014
DOI: 10.1038/nsmb.2152

実験手法

X-RAY DIFFRACTION (2.5 Å)