1y3a
From Proteopedia
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Structure of G-Alpha-I1 bound to a GDP-selective peptide provides insight into guanine nucleotide exchange
Overview
Heterotrimeric G proteins are molecular switches that regulate numerous, signaling pathways involved in cellular physiology. This characteristic is, achieved by the adoption of two principal states: an inactive, GDP bound, state and an active, GTP bound state. Under basal conditions, G proteins, exist in the inactive, GDP bound state; thus, nucleotide exchange is, crucial to the onset of signaling. Despite our understanding of G protein, signaling pathways, the mechanism of nucleotide exchange remains elusive., We employed phage display technology to identify nucleotide, state-dependent Galpha binding peptides. Herein, we report a GDP-selective, Galpha binding peptide, KB-752, that enhances spontaneous nucleotide, exchange of Galpha(i) subunits. Structural determination of the, Galpha(i1)/peptide complex reveals unique changes in the Galpha switch, regions predicted to enhance nucleotide exchange by creating a GDP, dissociation route. Our results cast light onto a potential mechanism by, which Galpha subunits adopt a conformation suitable for nucleotide, exchange.
About this Structure
1Y3A is a Single protein structure of sequence from Homo sapiens with GDP as ligand. Full crystallographic information is available from OCA.
Reference
Structure of Galpha(i1) bound to a GDP-selective peptide provides insight into guanine nucleotide exchange., Johnston CA, Willard FS, Jezyk MR, Fredericks Z, Bodor ET, Jones MB, Blaesius R, Watts VJ, Harden TK, Sondek J, Ramer JK, Siderovski DP, Structure. 2005 Jul;13(7):1069-80. PMID:16004878
Page seeded by OCA on Mon Nov 12 20:14:23 2007
