2ovn: Difference between revisions

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[[Image:2ovn.jpg|left|200px]]<br /><applet load="2ovn" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2ovn.jpg|left|200px]]
caption="2ovn" />
 
'''NMR structure of the GCN4 trigger peptide'''<br />
{{Structure
|PDB= 2ovn |SIZE=350|CAPTION= <scene name='initialview01'>2ovn</scene>
|SITE=  
|LIGAND=  
|ACTIVITY=  
|GENE=  
}}
 
'''NMR structure of the GCN4 trigger peptide'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2OVN is a [http://en.wikipedia.org/wiki/Single_protein 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].  
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].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17438295 17438295]
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:[http://www.ncbi.nlm.nih.gov/pubmed/17438295 17438295]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Alexandrescu, A T.]]
[[Category: Alexandrescu, A T.]]
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[[Category: trigger peptide]]
[[Category: trigger peptide]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:05:07 2008''

Revision as of 16:05, 20 March 2008

File:2ovn.jpg


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2ovn
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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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