1f5m
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(New page: 200px<br /><applet load="1f5m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f5m, resolution 1.9Å" /> '''STRUCTURE OF THE GAF ...)
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Revision as of 12:31, 20 November 2007
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STRUCTURE OF THE GAF DOMAIN
Overview
GAF domains are ubiquitous motifs present in cyclic GMP (cGMP)-regulated, cyclic nucleotide phosphodiesterases, certain adenylyl cyclases, the, bacterial transcription factor FhlA, and hundreds of other signaling and, sensory proteins from all three kingdoms of life. The crystal structure of, the Saccharomyces cerevisiae YKG9 protein was determined at 1.9 A, resolution. The structure revealed a fold that resembles the PAS domain, another ubiquitous signaling and sensory transducer. YKG9 does not bind, cGMP, but the isolated first GAF domain of phosphodiesterase 5 binds with, K:(d) = 650 nM. The cGMP binding site of the phosphodiesterase GAF domain, was identified by homology modeling and site-directed mutagenesis, and, consists of conserved Arg, Asn, Lys and Asp residues. The structural and, binding studies taken together show that the cGMP binding GAF domains form, a new class of cyclic nucleotide receptors distinct from the regulatory, domains of cyclic nucleotide-regulated protein kinases and ion channels.
About this Structure
1F5M is a Single protein structure of sequence from Saccharomyces cerevisiae with BR as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the GAF domain, a ubiquitous signaling motif and a new class of cyclic GMP receptor., Ho YS, Burden LM, Hurley JH, EMBO J. 2000 Oct 16;19(20):5288-99. PMID:11032796
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