Počet záznamů: 1
Implications for the active form of human insulin based on the structural convergence of highly active hormone analogues
- 1.0342433 - ÚOCHB 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. E-ISSN 1091-6490
Grant CEP: GA MŠMT(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
Počet záznamů: 1