1aot: Difference between revisions
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[[Category: signal transduction]] | [[Category: signal transduction]] | ||
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Revision as of 15:45, 30 October 2007
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NMR STRUCTURE OF THE FYN SH2 DOMAIN COMPLEXED WITH A PHOSPHOTYROSYL PEPTIDE, MINIMIZED AVERAGE STRUCTURE
OverviewOverview
BACKGROUND: SH2 domains are found in a variety of signal transduction, proteins; they bind phosphotyrosine-containing sequences, allowing them to, both recognize target molecules and regulate intramolecular kinase, activity. Fyn is a member of the Src family of tyrosine kinases that are, involved in signal transduction by association with a number of membrane, receptors. The kinase activity of these signalling proteins is modulated, by switching the binding mode of their SH2 and SH3 domains from, intramolecular to intermolecular. The molecular basis of the signalling, roles observed for different Src family members is still not well, understood; although structures have been determined for the SH2 domains, of other Src family molecules, this is the first structure of the Fyn SH2, domain. ... [(full description)]
About this StructureAbout this Structure
1AOT is a [Protein complex] structure of sequences from [Hamster polyomavirus] and [Homo sapiens]. Active as [Transferred entry: 2.7.10.1 and 2.7.10.2], with EC number [2.7.1.112]. Structure known Active Sites: 3IB and PTR. Full crystallographic information is available from [OCA].
ReferenceReference
The SH2 domain from the tyrosine kinase Fyn in complex with a phosphotyrosyl peptide reveals insights into domain stability and binding specificity., Mulhern TD, Shaw GL, Morton CJ, Day AJ, Campbell ID, Structure. 1997 Oct 15;5(10):1313-23. PMID:9351806
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