5KHQ

Rasip1 RA domain

5KHQ の概要

• エントリーDOI: 10.2210/pdb5khq/pdb
• 関連するPDBエントリー: 5KHO
• 分子名称: Ras-interacting protein 1, GLYCEROL (3 entities in total)
• 機能のキーワード: rasip1, ras-association domain, rap effector, signaling protein
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cytoplasm, perinuclear region : Q5U651
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32782.71

構造登録者

Gingras, A.R. (登録日: 2016-06-15, 公開日: 2016-10-19, 最終更新日: 2023-09-27)

主引用文献

Gingras, A.R.,Puzon-McLaughlin, W.,Bobkov, A.A.,Ginsberg, M.H.
Structural Basis of Dimeric Rasip1 RA Domain Recognition of the Ras Subfamily of GTP-Binding Proteins.
Structure, 24:2152-2162, 2016

PubMed Abstract: Ras-interacting protein 1 (Rasip1) is an endothelial-specific Rap1 and Ras effector, important for vascular development and angiogenesis. Here, we report the crystal structure of the Rasip1 RA domain (RRA) alone, revealing the basis of dimerization, and in complex with Rap1 at 2.8 Å resolution. In contrast to most RA domains, RRA formed a dimer that can bind two Rap1 (K = 0.9 μM) or Ras (K = 2.2 μM) molecules. We solved the Rap1-RRA complex and found that Rasip1 binds Rap1 in the Switch I region, and Rap1 binding induces few conformation changes to Rasip1 stabilizing a β strand and an unstructured loop. Our data explain how Rasip1 can act as a Rap1 and Ras effector and show that Rasip1 defines a subgroup of dimeric RA domains that could mediate cooperative binding to membrane-associated Ras superfamily members.

PubMed: 27839947
DOI: 10.1016/j.str.2016.10.001

実験手法

X-RAY DIFFRACTION (2.8 Å)