2q1v
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(New page: 200px<br /><applet load="2q1v" size="350" color="white" frame="true" align="right" spinBox="true" caption="2q1v, resolution 1.95Å" /> '''Ancestral corticoid ...)
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Revision as of 10:57, 23 January 2008
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Ancestral corticoid receptor in complex with cortisol
Overview
The structural mechanisms by which proteins have evolved new functions are, known only indirectly. We report x-ray crystal structures of a resurrected, ancestral protein-the ~450 million-year-old precursor of vertebrate, glucocorticoid (GR) and mineralocorticoid (MR) receptors. Using, structural, phylogenetic, and functional analysis, we identify the, specific set of historical mutations that recapitulate the evolution of, GR's hormone specificity from an MR-like ancestor. These substitutions, repositioned crucial residues to create new receptor-ligand and, intraprotein contacts. Strong epistatic interactions occur because one, substitution changes the conformational position of another site., "Permissive" mutations-substitutions of no immediate consequence, which, stabilize specific elements of the protein and allow it to tolerate, subsequent function-switching changes-played a major role in determining, GR's evolutionary trajectory.
About this Structure
2Q1V is a Protein complex structure of sequences from Unidentified with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal Structure of an Ancient Protein: Evolution by Conformational Epistasis., Ortlund EA, Bridgham JT, Redinbo MR, Thornton JW, Science. 2007 Aug 16;. PMID:17702911
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