1kjy
From Proteopedia
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'''Crystal Structure of Human G[alpha]i1 Bound to the GoLoco Motif of RGS14''' | '''Crystal Structure of Human G[alpha]i1 Bound to the GoLoco Motif of RGS14''' | ||
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[[Category: Siderovski, D P.]] | [[Category: Siderovski, D P.]] | ||
[[Category: Sondek, J.]] | [[Category: Sondek, J.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:50:00 2008'' | |
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Revision as of 19:50, 2 May 2008
Crystal Structure of Human G[alpha]i1 Bound to the GoLoco Motif of RGS14
Overview
Heterotrimeric G-proteins bind to cell-surface receptors and are integral in transmission of signals from outside the cell. Upon activation of the Galpha subunit by binding of GTP, the Galpha and Gbetagamma subunits dissociate and interact with effector proteins for signal transduction. Regulatory proteins with the 19-amino-acid GoLoco motif can bind to Galpha subunits and maintain G-protein subunit dissociation in the absence of Galpha activation. Here we describe the structural determinants of GoLoco activity as revealed by the crystal structure of Galpha(i1) GDP bound to the GoLoco region of the 'regulator of G-protein signalling' protein RGS14. Key contacts are described between the GoLoco motif and Galpha protein, including the extension of GoLoco's highly conserved Asp/Glu-Gln-Arg triad into the nucleotide-binding pocket of Galpha to make direct contact with the GDP alpha- and beta-phosphates. The structural organization of the GoLoco Galpha(i1) complex, when combined with supporting data from domain-swapping experiments, suggests that the Galpha all-helical domain and GoLoco-region carboxy-terminal residues control the specificity of GoLoco Galpha interactions.
About this Structure
1KJY is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural determinants for GoLoco-induced inhibition of nucleotide release by Galpha subunits., Kimple RJ, Kimple ME, Betts L, Sondek J, Siderovski DP, Nature. 2002 Apr 25;416(6883):878-81. PMID:11976690 Page seeded by OCA on Fri May 2 22:50:00 2008
