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| - | [[Image:1xhm.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1xhm| PDB=1xhm | SCENE= }} | | {{STRUCTURE_1xhm| PDB=1xhm | SCENE= }} |
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| - | '''The Crystal Structure of a Biologically Active Peptide (SIGK) Bound to a G Protein Beta:Gamma Heterodimer'''
| + | ===The Crystal Structure of a Biologically Active Peptide (SIGK) Bound to a G Protein Beta:Gamma Heterodimer=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16060668}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16060668 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16060668}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Protein-peptide complex]] | | [[Category: Protein-peptide complex]] |
| | [[Category: Wd40 repeat]] | | [[Category: Wd40 repeat]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:02:37 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:22:29 2008'' |
Revision as of 14:22, 27 July 2008
Template:STRUCTURE 1xhm
The Crystal Structure of a Biologically Active Peptide (SIGK) Bound to a G Protein Beta:Gamma Heterodimer
Template:ABSTRACT PUBMED 16060668
About this Structure
1XHM is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Jul 27 17:22:29 2008
