2J06
Crystal structure of the RasGAP SH3 domain at 1.8 Angstrom resolution
2J06 の概要
| エントリーDOI | 10.2210/pdb2j06/pdb |
| 関連するPDBエントリー | 1WER 1WQ1 2J05 |
| 分子名称 | RAS GTPASE-ACTIVATING PROTEIN 1 (2 entities in total) |
| 機能のキーワード | gtpase activation, sh3 domain, sh2 domain, src homology 3, ras signaling pathway, gtpase activating protein, proto-oncogene, phosphorylation, disease mutation, signal transduction |
| 由来する生物種 | HOMO SAPIENS (HUMAN) |
| 細胞内の位置 | Cytoplasm: P20936 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 15530.67 |
| 構造登録者 | |
| 主引用文献 | Ross, B.,Kristensen, O.,Favre, D.,Walicki, J.,Kastrup, J.S.,Widmann, C.,Gajhede, M. High Resolution Crystal Structures of the P120 Rasgap SH3 Domain. Biochem.Biophys.Res.Commun., 353:463-, 2007 Cited by PubMed Abstract: X-ray structures of two crystal forms of the Src homology 3 domain (SH3) of the Ras GTPase activating protein (RasGAP) were determined at 1.5 and 1.8A resolution. The overall structure comprises a single domain with two tightly packed beta-sheets linked by a short helical segment. An important motif for peptide binding in other SH3 domains is not conserved in RasGAP. The RasGAP SH3 domain forms dimers in the crystal structures, which may provide new functional insight. The dimer interface involves residues also present in a peptide previously identified as an apoptotic sensitizer of tumor cells. PubMed: 17188236DOI: 10.1016/J.BBRC.2006.12.044 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.8 Å) |
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