2ovn: Difference between revisions

Line 1:

[[~~Image~~:2ovn.~~png|left|200px~~]]

==NMR structure of the GCN4 trigger peptide==

== Structural highlights ==

<table><tr><td colspan='2'>[[2ovn]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OVN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OVN FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=2ovn RCSB], [http://www.ebi.ac.uk/pdbsum/2ovn PDBsum]</span></td></tr>

</table>

== 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.

~~{{STRUCTURE_2ovn| PDB=2ovn | SCENE= }}~~

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>

~~===NMR structure~~ of the ~~GCN4 trigger peptide===~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

~~{{ABSTRACT_PUBMED_17438295}}~~

== References ==

~~==About this Structure==~~

__TOC__

~~[[2ovn]] is a 1 chain structure~~. ~~Full experimental information is available from [http://oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=2OVN OCA].~~

</StructureSection>

==~~Reference~~==

<~~ref group="xtra">PMID:017438295<~~/~~ref~~><~~references group="xtra"~~/>

[[Category: Alexandrescu, A T.]]

[[Category: Matousek, W M.]]

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@@ Line 1: / Line 1: @@
-[[Image:2ovn.png|left|200px]]
+==NMR structure of the GCN4 trigger peptide==
+<StructureSection load='2ovn' size='340' side='right' caption='[[2ovn]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2ovn]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OVN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OVN FirstGlance]. <br>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=2ovn RCSB], [http://www.ebi.ac.uk/pdbsum/2ovn PDBsum]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== 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.
-{{STRUCTURE_2ovn|  PDB=2ovn  |  SCENE=  }}
+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>
-===NMR structure of the GCN4 trigger peptide===
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-{{ABSTRACT_PUBMED_17438295}}
+== References ==
+<references/>
-==About this Structure==
+__TOC__
-[[2ovn]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OVN OCA].
+</StructureSection>
-==Reference==
-<ref group="xtra">PMID:017438295</ref><references group="xtra"/>
 [[Category: Alexandrescu, A T.]]
 [[Category: Matousek, W M.]]