5JD0

crystal structure of ARAP3 RhoGAP domain

5JD0 の概要

• エントリーDOI: 10.2210/pdb5jd0/pdb
• 関連するPDBエントリー: 5JCP
• 分子名称: Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 3 (2 entities in total)
• 機能のキーワード: arap3, rhogap, signaling protein
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cytoplasm : Q8WWN8
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 48371.56

構造登録者

Bao, H.,Li, F.,Wu, J.,Shi, Y. (登録日: 2016-04-15, 公開日: 2016-06-22, 最終更新日: 2023-11-08)

主引用文献

Bao, H.,Li, F.,Wang, C.,Wang, N.,Jiang, Y.,Tang, Y.,Wu, J.,Shi, Y.
Structural Basis for the Specific Recognition of RhoA by the Dual GTPase-activating Protein ARAP3
J.Biol.Chem., 291:16709-16719, 2016

PubMed Abstract: ARAP3 (Arf-GAP with Rho-GAP domain, ANK repeat, and PH domain-containing protein 3) is unique for its dual specificity GAPs (GTPase-activating protein) activity for Arf6 (ADP-ribosylation factor 6) and RhoA (Ras homolog gene family member A) regulated by phosphatidylinositol 3,4,5-trisphosphate and a small GTPase Rap1-GTP and is involved in regulation of cell shape and adhesion. However, the molecular interface between the ARAP3-RhoGAP domain and RhoA is unknown, as is the substrates specificity of the RhoGAP domain. In this study, we solved the crystal structure of RhoA in complex with the RhoGAP domain of ARAP3. The structure of the complex presented a clear interface between the RhoGAP domain and RhoA. By analyzing the crystal structure and in combination with in vitro GTPase activity assays and isothermal titration calorimetry experiments, we identified the crucial residues affecting RhoGAP activity and substrates specificity among RhoA, Rac1 (Ras-related C3 botulinum toxin substrate 1), and Cdc42 (cell division control protein 42 homolog).

PubMed: 27311713
DOI: 10.1074/jbc.M116.736140

実験手法

X-RAY DIFFRACTION (2.3 Å)