1u3o
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(New page: 200px<br /><applet load="1u3o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u3o" /> '''Solution structure of rat Kalirin N-terminal...)
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Revision as of 01:42, 21 November 2007
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Solution structure of rat Kalirin N-terminal SH3 domain
Overview
RhoGEFs are central controllers of small G-proteins in cells and are, regulated by several mechanisms. There are at least 22 human RhoGEFs that, contain SH3 domains, raising the possibility that, like several other, enzymes, SH3 domains control the enzymatic activity of guanine nucleotide, exchange factor (GEF) domains through intra- and/or intermolecular, interactions. The structure of the N-terminal SH3 domain of Kalirin was, solved using NMR spectroscopy, and it folds much like other SH3 domains., However, NMR chemical shift mapping experiments showed that this Kalirin, SH3 domain is unique, containing novel cooperative binding site(s) for, intramolecular PXXP ligands. Intramolecular Kalirin SH3 domain/ligand, interactions, as well as binding of the Kalirin SH3 domain to the adaptor, protein Crk, inhibit the GEF activity of Kalirin. This study establishes a, novel molecular mechanism whereby intramolecular and intermolecular, Kalirin SH3 domain/ligand interactions modulate GEF activity, a regulatory, mechanism that is likely used by other RhoGEF family members.
About this Structure
1U3O is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Regulation of RhoGEF activity by intramolecular and intermolecular SH3 domain interactions., Schiller MR, Chakrabarti K, King GF, Schiller NI, Eipper BA, Maciejewski MW, J Biol Chem. 2006 Jul 7;281(27):18774-86. Epub 2006 Apr 27. PMID:16644733
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