1xhm

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Revision as of 06:57, 21 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1xhm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xhm, resolution 2.70Å" /> '''The Crystal Structur...)
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File:1xhm.gif


1xhm, resolution 2.70Å

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The Crystal Structure of a Biologically Active Peptide (SIGK) Bound to a G Protein Beta:Gamma Heterodimer

OverviewOverview

G protein betagamma subunits associate with many binding partners in, cellular signaling cascades. In previous work, we used random-peptide, phage display screening to identify a diverse family of peptides that, bound to a common surface on Gbetagamma subunits and blocked a subset of, Gbetagamma effectors. Later studies showed that one of the peptides caused, G protein activation through a novel Gbetagamma-dependent, nucleotide, exchange-independent mechanism. Here we report the X-ray crystal structure, of Gbeta(1)gamma(2) bound to this peptide, SIGK (SIGKAFKILGYPDYD), at 2.7, A resolution. SIGK forms a helical structure that binds the same face of, Gbeta(1) as the switch II region of Galpha. The interaction interface can, be subdivided into polar and nonpolar interfaces that together contain a, mixture of binding determinants that may be responsible for the ability of, this surface to recognize multiple protein partners. Systematic mutagenic, analysis of the peptide-Gbeta(1) interface indicates that distinct sets of, amino acids within this interface are required for binding of different, peptides. Among these unique amino acid interactions, specific, electrostatic binding contacts within the polar interface are required for, peptide-mediated subunit dissociation. The data provide a mechanistic, basis for multiple target recognition by Gbetagamma subunits with diverse, functional interactions within a common interface and suggest that, pharmacological targeting of distinct regions within this interface could, allow for selective manipulation of Gbetagamma-dependent signaling, pathways.

About this StructureAbout this Structure

1XHM is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Structural and molecular characterization of a preferred protein interaction surface on G protein beta gamma subunits., Davis TL, Bonacci TM, Sprang SR, Smrcka AV, Biochemistry. 2005 Aug 9;44(31):10593-604. PMID:16060668

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