4nj2: Difference between revisions

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-'''Unreleased structure'''
+==GCN4-p1 triple Val9, 23,30 to Ile mutant==
+<StructureSection load='4nj2' size='340' side='right' caption='[[4nj2]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4nj2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NJ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NJ2 FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene><br>
+<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
+<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zta|2zta]], [[4dmd|4dmd]], [[4niz|4niz]], [[4nj0|4nj0]], [[4nj1|4nj1]]</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=4nj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nj2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nj2 RCSB], [http://www.ebi.ac.uk/pdbsum/4nj2 PDBsum]</span></td></tr>
+<table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Nature uses proteins and nucleic acids to form a wide array of functional architectures, and scientists have found inspiration from these structures in the rational design of synthetic biomaterials. We have recently shown that a modular subunit consisting of two alpha-helical coiled coil peptides attached at their midpoints by an organic linking group can spontaneously self-assemble in aqueous solution to form a soluble supramolecular polymer. Here we explore the use of coiled-coil association affinity, readily tuned by amino acid sequence, as a means to predictably alter properties of these supramolecular assemblies. A series of dimeric coiled-coil peptide sequences with identical quaternary folded structures but systematically altered folded stability were designed and biophysically characterized. The sequences were cross-linked to generate a series of branched, self-assembling biomacromolecular subunits. A clear relationship is observed between coiled-coil association affinity and apparent hydrodynamic diameter of the supramolecular polymers formed by these subunits. Our results provide a family of soluble supramolecular polymers of tunable size and well-characterized coiled-coil sequences that add to the library of building blocks available for use in the rational design of protein-based supramolecular biomaterials.
-The entry 4nj2 is ON HOLD  until Paper Publication
+Tuning assembly size in Peptide-based supramolecular polymers by modulation of subunit association affinity.,Oshaben KM, Horne WS Biomacromolecules. 2014 Apr 14;15(4):1436-42. doi: 10.1021/bm5000423. Epub 2014, Mar 17. PMID:24598042<ref>PMID:24598042</ref>
-Authors: Oshaben, K.M., Horne, W.S.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: GCN4-p1 triple Val9, 23,30 to Ile mutant
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Horne, W S.]]
+[[Category: Oshaben, K M.]]
+[[Category: Transcription]]