2ovn

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[[Image:2ovn.jpg|left|200px]]
 
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==NMR structure of the GCN4 trigger peptide==
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The line below this paragraph, containing "STRUCTURE_2ovn", creates the "Structure Box" on the page.
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<StructureSection load='2ovn' size='340' side='right'caption='[[2ovn]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2ovn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2OVN FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ovn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ovn OCA], [https://pdbe.org/2ovn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ovn RCSB], [https://www.ebi.ac.uk/pdbsum/2ovn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ovn ProSAT]</span></td></tr>
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{{STRUCTURE_2ovn| PDB=2ovn | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GCN4_YEAST GCN4_YEAST] Is a transcription factor that is responsible for the activation of more than 30 genes required for amino acid or for purine biosynthesis in response to amino acid or purine starvation. Binds and recognize the DNA sequence: 5'-TGA[CG]TCA-3'.
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<div style="background-color:#fffaf0;">
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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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'''NMR structure of the GCN4 trigger peptide'''
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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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==Overview==
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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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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2OVN is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OVN OCA].
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</div>
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<div class="pdbe-citations 2ovn" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17438295 17438295]
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*[[Gcn4 3D Structures|Gcn4 3D Structures]]
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[[Category: Single protein]]
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*[[Gnc4 3D Structures|Gnc4 3D Structures]]
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[[Category: Alexandrescu, A T.]]
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== References ==
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[[Category: Matousek, W M.]]
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<references/>
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[[Category: Coiled-coil]]
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__TOC__
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[[Category: Gcn4]]
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</StructureSection>
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[[Category: Trigger peptide]]
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[[Category: Large Structures]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:45:35 2008''
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Alexandrescu AT]]
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[[Category: Matousek WM]]

Current revision

NMR structure of the GCN4 trigger peptide

PDB ID 2ovn

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