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5ycu
From Proteopedia
(Difference between revisions)
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</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=5ycu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ycu OCA], [http://pdbe.org/5ycu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ycu RCSB], [http://www.ebi.ac.uk/pdbsum/5ycu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ycu ProSAT]</span></td></tr> | </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=5ycu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ycu OCA], [http://pdbe.org/5ycu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ycu RCSB], [http://www.ebi.ac.uk/pdbsum/5ycu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ycu ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <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> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5ycu" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 09:40, 13 February 2019
Domain swapped dimer of engineered hairpin loop1 mutant in Single-chain Monellin
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