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2ovn

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[[Image:2ovn.jpg|left|200px]]
[[Image:2ovn.jpg|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ovn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ovn OCA], [http://www.ebi.ac.uk/pdbsum/2ovn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ovn RCSB]</span>
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'''NMR structure of the GCN4 trigger peptide'''
'''NMR structure of the GCN4 trigger peptide'''
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==About this Structure==
==About this Structure==
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2OVN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OVN OCA].
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2OVN is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OVN OCA].
==Reference==
==Reference==
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[[Category: Alexandrescu, A T.]]
[[Category: Alexandrescu, A T.]]
[[Category: Matousek, W M.]]
[[Category: Matousek, W M.]]
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[[Category: coiled-coil]]
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[[Category: Coiled-coil]]
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[[Category: gcn4]]
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[[Category: Gcn4]]
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[[Category: trigger peptide]]
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[[Category: Trigger peptide]]
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Revision as of 08:45, 4 May 2008

Template:STRUCTURE 2ovn

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. 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 Page seeded by OCA on Sun May 4 11:45:35 2008

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