2l56: Difference between revisions

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[[Image:2l56.png|left|200px]]
==NMR structure of the GCN4 trigger peptide refined using biased molecular dynamics simulations==
<StructureSection load='2l56' size='340' side='right' caption='[[2l56]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
== Structural highlights ==
[[2l56]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L56 OCA]. <br>
<b>Related:</b> [[2ovn|2ovn]]<br>
<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
== Publication Abstract from PubMed ==
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.


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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<ref>PMID:17438295</ref>
The line below this paragraph, containing "STRUCTURE_2l56", creates the "Structure Box" on the page.
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{{STRUCTURE_2l56|  PDB=2l56  |  SCENE=  }}


===NMR structure of the GCN4 trigger peptide refined using biased molecular dynamics simulations===
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
 
== References ==
 
<references/>
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==About this Structure==
[[2l56]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L56 OCA].
 
==Reference==
<ref group="xtra">PMID:017438295</ref><ref group="xtra">PMID:020954244</ref><references group="xtra"/>
[[Category: Dolenc, J.]]
[[Category: Dolenc, J.]]
[[Category: Gunsteren, W F.van.]]
[[Category: Gunsteren, W F.van.]]

Revision as of 08:39, 30 April 2014

NMR structure of the GCN4 trigger peptide refined using biased molecular dynamics simulations

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