2l56

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[[Image:2l56.png|left|200px]]
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==NMR structure of the GCN4 trigger peptide refined using biased molecular dynamics simulations==
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<StructureSection load='2l56' size='340' side='right' caption='[[2l56]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
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== Structural highlights ==
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[[2l56]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L56 OCA]. <br>
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<b>Related:</b> [[2ovn|2ovn]]<br>
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<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>
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== Publication Abstract from PubMed ==
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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>
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The line below this paragraph, containing "STRUCTURE_2l56", creates the "Structure Box" on the page.
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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or leave the SCENE parameter empty for the default display.
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{{STRUCTURE_2l56| PDB=2l56 | SCENE= }}
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===NMR structure of the GCN4 trigger peptide refined using biased molecular dynamics simulations===
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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== References ==
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_17438295}}, adds the Publication Abstract to the page
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</StructureSection>
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(as it appears on PubMed at http://www.pubmed.gov), where 17438295 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17438295}}
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==About this Structure==
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[[2l56]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L56 OCA].
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==Reference==
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<ref group="xtra">PMID:017438295</ref><ref group="xtra">PMID:020954244</ref><references group="xtra"/>
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[[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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