1DBH
DBL AND PLECKSTRIN HOMOLOGY DOMAINS FROM HSOS1
Summary for 1DBH
| Entry DOI | 10.2210/pdb1dbh/pdb |
| Descriptor | PROTEIN (HUMAN SOS 1) (2 entities in total) |
| Functional Keywords | guanine nucleotide exchange factor, gene regulation |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 41312.81 |
| Authors | Soisson, S.M.,Kuriyan, J. (deposition date: 1998-12-17, release date: 1998-12-23, Last modification date: 2024-11-13) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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