2ovn
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(New page: 200px<br /><applet load="2ovn" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ovn" /> '''NMR structure of the GCN4 trigger peptide'''...)
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Revision as of 13:05, 23 January 2008
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NMR structure of the GCN4 trigger peptide
Overview
Coiled coils have attracted considerable interest as design templates in a, wide range of applications. Successful coiled-coil design strategies, therefore require a detailed understanding of coiled-coil folding. One, common feature shared by coiled coils is the presence of a short, autonomous helical folding unit, termed "trigger sequence," that is, indispensable for folding. Detailed knowledge of trigger sequences at the, molecular level is thus key to a general understanding of coiled-coil, formation. Using a multidisciplinary approach, we identify and, characterize here the molecular determinants that specify the helical, conformation of the monomeric early folding intermediate of the GCN4, coiled coil. We demonstrate that a network of hydrogen-bonding and, electrostatic interactions stabilize the trigger-sequence helix. This, network is rearranged in the final dimeric coiled-coil structure, and its, destabilization significantly slows down GCN4 leucine zipper folding. Our, findings provide a general explanation for the molecular mechanism of, coiled-coil formation.
About this Structure
2OVN is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Molecular basis of coiled-coil formation., Steinmetz MO, Jelesarov I, Matousek WM, Honnappa S, Jahnke W, Missimer JH, Frank S, Alexandrescu AT, Kammerer RA, Proc Natl Acad Sci U S A. 2007 Apr 24;104(17):7062-7. Epub 2007 Apr 16. PMID:17438295
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