2q1v
From Proteopedia
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[[Image:2q1v.jpg|left|200px]] | [[Image:2q1v.jpg|left|200px]] | ||
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'''Ancestral corticoid receptor in complex with cortisol''' | '''Ancestral corticoid receptor in complex with cortisol''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q1V OCA]. | |
==Reference== | ==Reference== | ||
Crystal structure of an ancient protein: evolution by conformational epistasis., Ortlund EA, Bridgham JT, Redinbo MR, Thornton JW, Science. 2007 Sep 14;317(5844):1544-8. Epub 2007 Aug 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17702911 17702911] | Crystal structure of an ancient protein: evolution by conformational epistasis., Ortlund EA, Bridgham JT, Redinbo MR, Thornton JW, Science. 2007 Sep 14;317(5844):1544-8. Epub 2007 Aug 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17702911 17702911] | ||
| - | [[Category: Protein complex]] | ||
| - | [[Category: Unidentified]] | ||
[[Category: Ortlund, E A.]] | [[Category: Ortlund, E A.]] | ||
[[Category: Redinbo, M R.]] | [[Category: Redinbo, M R.]] | ||
| - | [[Category: | + | [[Category: Common ancestor]] |
| - | [[Category: | + | [[Category: Corticoid]] |
| - | [[Category: | + | [[Category: Cortisol]] |
| - | [[Category: | + | [[Category: Evolution]] |
| - | [[Category: | + | [[Category: Mineralocorticoid]] |
| - | [[Category: | + | [[Category: Nuclear receptor]] |
| - | [[Category: | + | [[Category: Transcription]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:11:22 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 11:11, 4 May 2008
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 approximately 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
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 Sep 14;317(5844):1544-8. Epub 2007 Aug 16. PMID:17702911 Page seeded by OCA on Sun May 4 14:11:22 2008
