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Titolo:
Crystal structure of the complex of Brugia malayi cyclophilin and cyclosporin A
Autore:
Ellis, PJ; Carlow, CKS; Ma, D; Kuhn, P;
Indirizzi:
Stanford Univ, Stanford Linear Accelerator Ctr, Stanford Synchrotron Radiat Lab, Stanford, CA 94309 USA Stanford Univ Stanford CA USA 94309 on Radiat Lab, Stanford, CA 94309 USA New England Biolabs Inc, Beverly, MA 01915 USA New England Biolabs Inc Beverly MA USA 01915 s Inc, Beverly, MA 01915 USA
Titolo Testata:
BIOCHEMISTRY
fascicolo: 3, volume: 39, anno: 2000,
pagine: 592 - 598
SICI:
0006-2960(20000125)39:3<592:CSOTCO>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
A-INSENSITIVE CYCLOPHILIN; X-RAY STRUCTURE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
21
Recensione:
Indirizzi per estratti:
Indirizzo: Kuhn, P Stanford Univ, Stanford Linear Accelerator Ctr, Stanford Synchrotron Radiat Lab, POB 4249,Bin 69, Stanford, CA 94309 USA Stanford Univ POB 4249,Bin 69 Stanford CA USA 94309 , CA 94309 USA
Citazione:
P.J. Ellis et al., "Crystal structure of the complex of Brugia malayi cyclophilin and cyclosporin A", BIOCHEM, 39(3), 2000, pp. 592-598

Abstract

The resistance of the human parasite Brugia malayi to the antiparasitic activity of cyclosporin A (CsA) may arise from the presence of cyclophilins with relatively low affinity for the drug. The structure of the complex of B. malayi cyclophilin (BmCYP-1) and CsA, with eight independent copies in the asymmetric unit, has been determined at a resolution of 2.7 Angstrom. Thelow affinity of BmCYP-1 for CsA arises from incomplete preorganization of the binding site so that the formation of a hydrogen bond between His132 ofBmCYP-1 and N-methylleucine 9 of CsA is associated with a shift in the backbone of approximately 1 Angstrom in this region.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/11/20 alle ore 17:21:55