1jun: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1jun]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JUN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JUN FirstGlance]. <br> | <table><tr><td colspan='2'>[[1jun]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JUN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JUN FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jun OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jun RCSB], [http://www.ebi.ac.uk/pdbsum/1jun PDBsum]</span></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=1jun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jun OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jun RCSB], [http://www.ebi.ac.uk/pdbsum/1jun PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Donoghue, S I.O | [[Category: Donoghue, S I.O]] | ||
[[Category: Junius, F K | [[Category: Junius, F K]] | ||
[[Category: King, G F | [[Category: King, G F]] | ||
[[Category: Nilges, M | [[Category: Nilges, M]] | ||
[[Category: Dna-binding regulatory protein]] | [[Category: Dna-binding regulatory protein]] | ||
[[Category: Oncogene protein]] | [[Category: Oncogene protein]] | ||
[[Category: Transcription activation]] | [[Category: Transcription activation]] | ||
[[Category: Transcription regulation]] | [[Category: Transcription regulation]] | ||
Revision as of 15:04, 2 January 2015
NMR STUDY OF C-JUN HOMODIMERNMR STUDY OF C-JUN HOMODIMER
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe solution structure of the c-Jun leucine zipper domain has been determined to high resolution using a new calculation protocol designed to handle highly ambiguous sets of interproton distance restraints. The domain comprises a coiled coil of parallel alpha-helices in which most of the hydrophobic residues are buried at the highly symmetrical dimer interface; this interface extends over 10 helical turns and is the most elongated protein domain solved to date using NMR methods. The backbone fold is very similar to that seen in crystal structures of the GCN4 and Jun-Fos leucine zippers; however, in contrast with these crystal structures, the Jun leucine zipper dimer appears to be devoid of favorable intermolecular electrostatic interactions. A polar asparagine residue, located at the dimer interface, forms the sole point of asymmetry in the structure; furthermore, the side chain of this residue is disordered due to motional averaging. This residue, which is highly conserved in the leucine zipper family of transcription factors, provides a destabilizing influence that is likely to facilitate the rapid exchange of zipper strands in vivo. High resolution NMR solution structure of the leucine zipper domain of the c-Jun homodimer.,Junius FK, O'Donoghue SI, Nilges M, Weiss AS, King GF J Biol Chem. 1996 Jun 7;271(23):13663-7. PMID:8662824[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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