5k86
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Aza-glycine containing collagen peptide== | |
| + | <StructureSection load='5k86' size='340' side='right'caption='[[5k86]], [[Resolution|resolution]] 1.13Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5k86]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K86 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K86 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.127Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=XZA:diazanecarboxylic+acid'>XZA</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5k86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k86 OCA], [https://pdbe.org/5k86 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k86 RCSB], [https://www.ebi.ac.uk/pdbsum/5k86 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k86 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Previously, we have demonstrated that replacement of the strictly conserved glycine in collagen with aza-glycine provides a general solution for stabilizing triple helical collagen peptides (Chenoweth, D. M.; et al. J. Am. Chem. Soc. 2016, 138, 9751 ; 2015, 137, 12422 ). The additional hydrogen bond and conformational constraints provided by aza-glycine increases the thermal stability and rate of folding in collagen peptides composed of Pro-Hyp-Gly triplet repeats, allowing for truncation to the smallest self-assembling peptide systems observed to date. Here we show that aza-glycine substitution enhances the stability of an arginine-containing collagen peptide and provide a structural basis for this stabilization with an atomic resolution crystal structure. These results demonstrate that a single nitrogen atom substitution for a glycine alpha-carbon increases the peptide's triple helix melting temperature by 8.6 degrees C. Furthermore, we provide the first structural basis for stabilization of triple helical collagen peptides containing aza-glycine and we demonstrate that minimal alteration to the peptide backbone conformation occurs with aza-glycine incorporation. | ||
| - | + | Structural Basis for Aza-Glycine Stabilization of Collagen.,Kasznel AJ, Zhang Y, Hai Y, Chenoweth DM J Am Chem Soc. 2017 Jul 19;139(28):9427-9430. doi: 10.1021/jacs.7b03398. Epub, 2017 Jul 6. PMID:28650147<ref>PMID:28650147</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5k86" style="background-color:#fffaf0;"></div> |
| - | [[Category: Chenoweth | + | == References == |
| - | [[Category: Hai | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Synthetic construct]] | ||
| + | [[Category: Chenoweth DM]] | ||
| + | [[Category: Hai Y]] | ||
| + | [[Category: Kasznel AJ]] | ||
Current revision
Aza-glycine containing collagen peptide
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