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2ovn
From Proteopedia
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| - | [[Image:2ovn.jpg|left|200px]] | + | [[Image:2ovn.jpg|left|200px]] |
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| - | '''NMR structure of the GCN4 trigger peptide''' | + | {{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 [ | + | 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:// | + | 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]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''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
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
Page seeded by OCA on Thu Mar 20 18:05:07 2008
