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2ww7
From Proteopedia
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| - | [[ | + | ==FOLDON CONTAINING BETA-TURN MIMIC== |
| + | <StructureSection load='2ww7' size='340' side='right' caption='[[2ww7]], [[Resolution|resolution]] 1.06Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2ww7]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WW7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WW7 FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=NA8:(1S)-1-CARBOXY-2-NAPHTHALEN-2-YLETHANAMINIUM'>NA8</scene>, <scene name='pdbligand=PRS:THIOPROLINE'>PRS</scene>, <scene name='pdbligand=TH6:4-HYDROXY-L-THREONINE'>TH6</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ww6|2ww6]]</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=2ww7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ww7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ww7 RCSB], [http://www.ebi.ac.uk/pdbsum/2ww7 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | beta-Turns are secondary structure elements not only exposed on protein surfaces, but also frequently found to be buried in protein-protein interfaces. Protein engineering so far considered mainly the backbone-constraining properties of synthetic beta-turn mimics as parts of surface-exposed loops. A beta-turn mimic, Hot horizontal lineTap, that is available in gram amounts, provides two hydroxyl groups that enhance its turn-inducing properties besides being able to form side-chain-like interactions. NMR studies on cyclic hexapeptides harboring the Hot horizontal lineTap dipeptide proved its strong beta-turn-inducing capability. Crystallographic analyses of the trimeric fibritin-foldon/Hot horizontal lineTap hybrid reveal at atomic resolution how Hot horizontal lineTap replaces a betaI'-turn by a betaII'-type structure. Furthermore, Hot horizontal lineTap adapts to the complex protein environment by participating in several direct and water-bridged interactions across the foldon trimer interface. As building blocks, beta-turn mimics capable of both backbone and side-chain mimicry may simplify the design of synthetic proteins. | ||
| - | + | Structural characterization of a beta-turn mimic within a protein-protein interface.,Eckhardt B, Grosse W, Essen LO, Geyer A Proc Natl Acad Sci U S A. 2010 Oct 26;107(43):18336-41. Epub 2010 Oct 11. PMID:20937907<ref>PMID:20937907</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| - | + | ==See Also== | |
| - | + | *[[Fibritin|Fibritin]] | |
| - | == | + | == References == |
| - | [[ | + | <references/> |
| - | + | __TOC__ | |
| - | == | + | </StructureSection> |
| - | < | + | |
[[Category: Eckhardt, B.]] | [[Category: Eckhardt, B.]] | ||
[[Category: Essen, L O.]] | [[Category: Essen, L O.]] | ||
Revision as of 12:49, 22 October 2014
FOLDON CONTAINING BETA-TURN MIMIC
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