1DBH
DBL AND PLECKSTRIN HOMOLOGY DOMAINS FROM HSOS1
1DBH の概要
| エントリーDOI | 10.2210/pdb1dbh/pdb |
| 分子名称 | PROTEIN (HUMAN SOS 1) (2 entities in total) |
| 機能のキーワード | guanine nucleotide exchange factor, gene regulation |
| 由来する生物種 | Homo sapiens (human) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 41312.81 |
| 構造登録者 | |
| 主引用文献 | Soisson, S.M.,Nimnual, A.S.,Uy, M.,Bar-Sagi, D.,Kuriyan, J. Crystal structure of the Dbl and pleckstrin homology domains from the human Son of sevenless protein. Cell(Cambridge,Mass.), 95:259-268, 1998 Cited by PubMed Abstract: Proteins containing Dbl homology (DH) domains activate Rho-family GTPases by functioning as specific guanine nucleotide exchange factors. All known DH domains have associated C-terminal pleckstrin homology (PH) domains that are implicated in targeting and regulatory functions. The crystal structure of a fragment of the human Son of sevenless protein containing the DH and PH domains has been determined at 2.3 A resolution. The entirely alpha-helical DH domain is unrelated in architecture to other nucleotide exchange factors. The active site of the DH domain, identified on the basis of sequence conservation and structural features, lies near the interface between the DH and PH domains. The structure suggests that ligation of the PH domain will be coupled structurally to the GTPase binding site. PubMed: 9790532DOI: 10.1016/S0092-8674(00)81756-0 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.3 Å) |
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