3BRW
Structure of the Rap-RapGAP complex
3BRW の概要
エントリーDOI | 10.2210/pdb3brw/pdb |
関連するPDBエントリー | 1SRQ |
分子名称 | Rap1 GTPase-activating protein 1, Ras-related protein Rap-1b, MAGNESIUM ION, ... (6 entities in total) |
機能のキーワード | gap, g proteins, gtpase, rap, gtpase activation, gtp-binding, gtp binding protein |
由来する生物種 | Homo sapiens (human) 詳細 |
細胞内の位置 | Golgi apparatus membrane; Peripheral membrane protein: P47736 Cell membrane: P61224 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 136257.77 |
構造登録者 | Scrima, A.,Thomas, C.,Deaconescu, D.,Wittinghofer, A. (登録日: 2007-12-21, 公開日: 2008-03-11, 最終更新日: 2023-11-01) |
主引用文献 | Scrima, A.,Thomas, C.,Deaconescu, D.,Wittinghofer, A. The Rap-RapGAP complex: GTP hydrolysis without catalytic glutamine and arginine residues Embo J., 27:1145-1153, 2008 Cited by PubMed Abstract: The GTP-binding protein Rap1 regulates integrin-mediated and other cell adhesion processes. Unlike most other Ras-related proteins, it contains a threonine in switch II instead of a glutamine (Gln61 in Ras), a residue crucial for the GTPase reaction of most G proteins. Furthermore, unlike most other GTPase-activating proteins (GAPs) for small G proteins, which supply a catalytically important Arg-finger, no arginine residue of RapGAP makes a significant contribution to the GTPase reaction of Rap1. For a detailed understanding of the reaction mechanism, we have solved the structure of Rap1 in complex with Rap1GAP. It shows that the Thr61 of Rap is away from the active site and that an invariant asparagine of RapGAPs, the Asn-thumb, takes over the role of the cis-glutamine of Ras, Rho or Ran. The structure and biochemical data allow to further explain the mechanism and to define the important role of a conserved tyrosine. The structure and biochemical data furthermore show that the RapGAP homologous region of the tumour suppressor Tuberin is sufficient for catalysis on Rheb. PubMed: 18309292DOI: 10.1038/emboj.2008.30 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.4 Å) |
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