View source for 5ycu


==Domain swapped dimer of engineered hairpin loop1 mutant in Single-chain Monellin==
<StructureSection load='5ycu' size='340' side='right'caption='[[5ycu]], [[Resolution|resolution]] 2.32&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ycu]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Dioscoreophyllum_cumminsii Dioscoreophyllum cumminsii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YCU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YCU 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]] 2.32&#8491;</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=5ycu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ycu OCA], [https://pdbe.org/5ycu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ycu RCSB], [https://www.ebi.ac.uk/pdbsum/5ycu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ycu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MONA_DIOCU MONA_DIOCU] Taste-modifying protein; intensely sweet-tasting protein.[https://www.uniprot.org/uniprot/MONB_DIOCU MONB_DIOCU] Taste-modifying protein; intensely sweet-tasting protein.
<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&reg;/PubMed&reg;, 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__
</StructureSection>
[[Category: Dioscoreophyllum cumminsii]]
[[Category: Large Structures]]
[[Category: Das R]]
[[Category: Gosavi S]]
[[Category: Nandwani N]]
[[Category: Surana P]]
[[Category: Udgaonkar JB]]