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Implications for the active form of human insulin based on the structural convergence of highly active hormone analogues
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SYSNO ASEP 0342433 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Implications for the active form of human insulin based on the structural convergence of highly active hormone analogues Author(s) Jiráček, Jiří (UOCHB-X) RID, ORCID
Žáková, Lenka (UOCHB-X) RID, ORCID
Antolíková, Emília (UOCHB-X)
Watson, C. J. (GB)
Turkenburg, J. P. (GB)
Dodson, G. G. (GB)
Brzozowski, A. M. (GB)Number of authors 7 Source Title Proceedings of the National Academy of Sciences of the United States of America. - : National Academy of Sciences - ISSN 0027-8424
Roč. 107, č. 5 (2010), s. 1966-1970Number of pages 5 s. Language eng - English Country US - United States Keywords insulin ; analogue ; conformation ; beta-turn ; N-methylation Subject RIV CC - Organic Chemistry R&D Projects LC06077 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) KJB400550702 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR) CEZ AV0Z40550506 - UOCHB-X (2005-2011) UT WOS 000274296300031 DOI 10.1073/pnas.0911785107 Annotation Here, we present the design and analysis of highly active (200–500%) insulin analogues that are truncated at residue 26 of the B-chain (B26). They show a structural convergence in the form of a new (beta)-turn at B24-B26. We propose that the key element in insulin’s transition, from an inactive to an active state, may be the formation of the (beta)-turn at B24-B26 associated with a trans to cis isomerisation at the B25-B26 peptide bond. 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 2011
Number of the records: 1