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001-es BibID:	BIBFORM040695
Első szerző:	Tőzsér József (molekuláris biológus, biokémikus, vegyész)
Cím:	Studies on the role of the S4 substrate binding site of HIV proteinases / Tözsér József, Gustchina Alla, Weber Irene T., Blaha Ivo, Wondrak Ewald M., Oroszlan Stephen
Dátum:	1991
ISSN:	0014-5793
Megjegyzések:	Kinetic analysis of the hydrolysis of the peptide H-Val-Ser-Gln-Asn-Tyr*Pro-Ile-Val-Gln-NH2 and its analogs obtained by varying the length and introducing substitutions at the P4 site was carried out with both HIV-1 and HIV-2 proteinases. Deletion of the terminal Val and Gln had only moderate effect on the substrate hydrolysis, while the deletion of the P4. Ser as well as P'3 Val greatly reduced the substrate hydrolysis. This is predicted to be due to the loss of interactions between main chains of the enzyme and the substrate. Substitution of the P4 Ser by amino acids having high frequency of occurrence in beta turns resulted in good substrates, while large amino acids were unfavorable in this position. The two proteinases acted similarly, except for substrates having Thr, Val and Leu substitutions, which were better accommodated in the HIV-2 substrate binding pocket.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Febs Letters. - 279 : 2 (1991), p. 356-360. -
További szerzők:	Gustchina, Alla Weber, Irene T. Bláha, Ivo Wondrak, Ewald M. Oroszlan, Stephen
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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