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High-resolution structure of a retroviral protease folded as a monomer
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SYSNO ASEP 0369861 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title High-resolution structure of a retroviral protease folded as a monomer Author(s) Gilski, M. (PL)
Kazmierczyk, M. (PL)
Krzywda, S. (PL)
Zábranská, Helena (UOCHB-X) RID
Cooper, S. (US)
Popovic, Z. (US)
Khatíb, F. (US)
Dímaio, F. (US)
Thompson, J. (US)
Baker, D. (US)
Pichová, Iva (UOCHB-X) RID, ORCID
Jaskolski, M. (PL)Number of authors 12 Source Title Acta Crystallographica Section D-Biological Crystallography. - : WILEY-BLACKWELL - ISSN 0907-4449
D67, č. 11 (2011), s. 907-914Number of pages 8 s. Language eng - English Country DK - Denmark Keywords M-PMV protease ; crystal structure ; monomer ; dimerization inhibitors Subject RIV CE - Biochemistry R&D Projects 1M0508 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) CEZ AV0Z40550506 - UOCHB-X (2005-2011) UT WOS 000296787400001 DOI 10.1107/S0907444911035943 Annotation Biophysical and NMR studies of M-PMV protease have indicated that in the absence of substrates or inhibitors M-PMV PR should fold into a stable monomer, but the crystal structure of this protein could not be solved by molecular replacement despite countless attempts. The solution was obtained in mr-rosetta using a model constructed by players of the game Foldit. The structure shows a monomeric protein, with the N- and C-termini completely disordered. The flap loop has an unusual curled shape and a different orientation from both the open and closed states known from dimeric retropepsins. This structure provides important information for the design of dimerization inhibitors of retroviral proteases. Workplace Institute of Organic Chemistry and Biochemistry Contact asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Viktorie Chládková, Tel.: 232 002 434 Year of Publishing 2012
Number of the records: 1