6idc
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Loop deletion and proline insertion mutant (deleting six residues and inserted six proline residues)== | |
| + | <StructureSection load='6idc' size='340' side='right'caption='[[6idc]], [[Resolution|resolution]] 2.01Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6idc]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IDC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IDC FirstGlance]. <br> | ||
| + | </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=6idc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6idc OCA], [http://pdbe.org/6idc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6idc RCSB], [http://www.ebi.ac.uk/pdbsum/6idc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6idc ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In "domain-swapping," proteins mutually interconvert structural elements to form a dimer/oligomer. Engineering this process by design is important for creating a higher order protein assembly with minimal modification. Herein, we show a simple design strategy for domain-swapping formation by loop deletion and insertion of a polyproline rod. Crystal structures revealed the formation of the domain-swapped dimers and the polyproline portion formed a polyproline II (PPII) structure. Small-angle x-ray scattering (SAXS) demonstrated that an extended orientation of domain-swapped dimer was retained in the solution. We found that a multiple of three of inserting proline residue is favored for domain-swapping because of the helical nature of PPII. The rigid nature of the polyproline rod enables precise control of the interdomain distance and orientation. | ||
| - | + | Domain-swapping design by poly-proline rod insertion.,Shiga S, Yamanaka M, Fujiwara W, Hirota S, Goda S, Makabe K Chembiochem. 2019 May 15. doi: 10.1002/cbic.201900179. PMID:31094059<ref>PMID:31094059</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6idc" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Makabe, K]] | ||
| + | [[Category: Shiga, S]] | ||
| + | [[Category: De novo protein]] | ||
| + | [[Category: Lipid binding protein]] | ||
| + | [[Category: Outer surface protein some]] | ||
Revision as of 05:49, 3 July 2019
Loop deletion and proline insertion mutant (deleting six residues and inserted six proline residues)
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