2ww6
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==foldon containing D-amino acids in turn positions== | |
| + | <StructureSection load='2ww6' size='340' side='right'caption='[[2ww6]], [[Resolution|resolution]] 0.98Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2ww6]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WW6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WW6 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]] 0.98Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=DPN:D-PHENYLALANINE'>DPN</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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=2ww6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ww6 OCA], [https://pdbe.org/2ww6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ww6 RCSB], [https://www.ebi.ac.uk/pdbsum/2ww6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ww6 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q76VI8_9CAUD Q76VI8_9CAUD] | ||
| + | <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> | ||
| + | <div class="pdbe-citations 2ww6" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| + | *[[Fibritin|Fibritin]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia virus T4]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Eckhardt B]] | ||
| + | [[Category: Essen L-O]] | ||
| + | [[Category: Geyer A]] | ||
| + | [[Category: Grosse W]] | ||
Current revision
foldon containing D-amino acids in turn positions
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