5u2l
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the Hsp104 N-terminal domain from Candida albicans== | |
| + | <StructureSection load='5u2l' size='340' side='right' caption='[[5u2l]], [[Resolution|resolution]] 1.66Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5u2l]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5U2L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5U2L 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=5u2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u2l OCA], [http://pdbe.org/5u2l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5u2l RCSB], [http://www.ebi.ac.uk/pdbsum/5u2l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5u2l ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Hsp104 is a yeast member of the Hsp100 family which functions as a molecular chaperone to disaggregate misfolded polypeptides. To understand the mechanism by which the Hsp104 N-terminal domain (NTD) interacts with its peptide substrates, crystal structures of the Hsp104 NTDs from Saccharomyces cerevisiae (ScHsp104NTD) and Candida albicans (CaHsp104NTD) have been determined at high resolution. The structures of ScHsp104NTD and CaHsp104NTD reveal that the yeast Hsp104 NTD may utilize a conserved putative peptide-binding groove to interact with misfolded polypeptides. In the crystal structures ScHsp104NTD forms a homodimer, while CaHsp104NTD exists as a monomer. The consecutive residues Gln105, Gln106 and Lys107, and Lys141 around the putative peptide-binding groove mediate the monomer-monomer interactions within the ScHsp104NTD homodimer. Dimer formation by ScHsp104NTD suggests that the Hsp104 NTD may specifically interact with polyQ regions of prion-prone proteins. The data may reveal the mechanism by which Hsp104 NTD functions to suppress and/or dissolve prions. | ||
| - | + | Crystal structures of Hsp104 N-terminal domains from Saccharomyces cerevisiae and Candida albicans suggest the mechanism for the function of Hsp104 in dissolving prions.,Wang P, Li J, Weaver C, Lucius A, Sha B Acta Crystallogr D Struct Biol. 2017 Apr 1;73(Pt 4):365-372. doi:, 10.1107/S2059798317002662. Epub 2017 Mar 31. PMID:28375147<ref>PMID:28375147</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5u2l" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Li, J]] | [[Category: Li, J]] | ||
| + | [[Category: Sha, B]] | ||
[[Category: Wang, P]] | [[Category: Wang, P]] | ||
| + | [[Category: Candida albican]] | ||
| + | [[Category: Hsp104]] | ||
| + | [[Category: N-terminal domain]] | ||
| + | [[Category: Protein binding]] | ||
Revision as of 13:03, 19 April 2017
Crystal structure of the Hsp104 N-terminal domain from Candida albicans
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