2ww7
From Proteopedia
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- | [[Image:2ww7.png|left|200px]] | ||
- | + | ==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 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=2WW7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WW7 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]] 1.06Å</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=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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ww7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ww7 OCA], [https://pdbe.org/2ww7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ww7 RCSB], [https://www.ebi.ac.uk/pdbsum/2ww7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ww7 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/Q76VI8_BPT2 Q76VI8_BPT2] | ||
+ | <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 2ww7" style="background-color:#fffaf0;"></div> | ||
- | == | + | ==See Also== |
- | [[ | + | *[[Fibritin|Fibritin]] |
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
- | [[Category: | + | </StructureSection> |
- | [[Category: | + | [[Category: Escherichia virus T4]] |
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: | + | [[Category: Eckhardt B]] |
- | [[Category: | + | [[Category: Essen L-O]] |
- | [[Category: | + | [[Category: Geyer A]] |
- | + | [[Category: Grosse W]] |
Current revision
foldon containing beta-turn mimic
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