Počet záznamů: 1

Implications for the active form of human insulin based on the structural convergence of highly active hormone analogues

  1. 1.
    0342433 - UOCHB-X 2011 RIV US eng J - Článek v odborném periodiku
    Jiráček, Jiří - Žáková, Lenka - Antolíková, Emília - Watson, C. J. - Turkenburg, J. P. - Dodson, G. G. - Brzozowski, A. M.
    Implications for the active form of human insulin based on the structural convergence of highly active hormone analogues.
    Proceedings of the National Academy of Sciences of the United States of America. Roč. 107, č. 5 (2010), s. 1966-1970 ISSN 0027-8424
    Grant CEP: GA MŠk(CZ) LC06077; GA AV ČR KJB400550702
    Výzkumný záměr: CEZ:AV0Z40550506
    Klíčová slova: insulin * analogue * conformation * beta-turn * N-methylation
    Kód oboru RIV: CC - Organická chemie
    Impakt faktor: 9.771, rok: 2010

    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.
    Trvalý link: http://hdl.handle.net/11104/0185172