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6iwj
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==A designed domain swapped dimer== | |
| + | <StructureSection load='6iwj' size='340' side='right'caption='[[6iwj]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6iwj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanopyrus_kandleri_AV19 Methanopyrus kandleri AV19]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IWJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IWJ FirstGlance]. <br> | ||
| + | </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=6iwj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iwj OCA], [https://pdbe.org/6iwj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6iwj RCSB], [https://www.ebi.ac.uk/pdbsum/6iwj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6iwj ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q8TYK3_METKA Q8TYK3_METKA] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Domain swapping is the process by which identical monomeric proteins exchange structural elements to generate dimers/oligomers. Although engineered domain swapping is a compelling strategy for protein assembly, its application has been limited due to the lack of simple and reliable design approaches. Here, we demonstrate that the hydrophobic five-residue 'cystatin motif' (QVVAG) from the domain-swapping protein Stefin B, when engineered into a solvent-exposed, tight surface loop between two beta-strands prevents the loop from folding back upon itself, and drives domain swapping in non-domain-swapping proteins. High-resolution structural studies demonstrate that engineering the QVVAG stretch independently into various surface loops of four structurally distinct non-domain-swapping proteins enabled the design of different modes of domain swapping in these proteins, including single, double and open-ended domain swapping. These results suggest that the introduction of the QVVAG motif can be used as a mutational approach for engineering domain swapping in diverse beta-hairpin proteins. | ||
| - | + | A five-residue motif for the design of domain swapping in proteins.,Nandwani N, Surana P, Negi H, Mascarenhas NM, Udgaonkar JB, Das R, Gosavi S Nat Commun. 2019 Jan 28;10(1):452. doi: 10.1038/s41467-019-08295-x. PMID:30692525<ref>PMID:30692525</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6iwj" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Methanopyrus kandleri AV19]] | ||
| + | [[Category: Das R]] | ||
| + | [[Category: Nandwani N]] | ||
| + | [[Category: Negi H]] | ||
Current revision
A designed domain swapped dimer
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