1dbh: Difference between revisions
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'''DBL AND PLECKSTRIN HOMOLOGY DOMAINS FROM HSOS1''' | '''DBL AND PLECKSTRIN HOMOLOGY DOMAINS FROM HSOS1''' | ||
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[[Category: Kuriyan, J.]] | [[Category: Kuriyan, J.]] | ||
[[Category: Soisson, S M.]] | [[Category: Soisson, S M.]] | ||
[[Category: | [[Category: Guanine nucleotide exchange factor]] | ||
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Revision as of 13:39, 2 May 2008
DBL AND PLECKSTRIN HOMOLOGY DOMAINS FROM HSOS1
OverviewOverview
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.
About this StructureAbout this Structure
1DBH is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the Dbl and pleckstrin homology domains from the human Son of sevenless protein., Soisson SM, Nimnual AS, Uy M, Bar-Sagi D, Kuriyan J, Cell. 1998 Oct 16;95(2):259-68. PMID:9790532 Page seeded by OCA on Fri May 2 13:39:32 2008