Mutating P2 and P1 residues at cleavage junctions in the HIV-1 pol polyprotein Effects on hydrolysis by HIV-1 proteinase

Mutations were introduced into the P2 and P1 positions of the junctions, (a) linking reverse transcriptase (RT) and integrase (IN) (-Leu*Phe-) and (b) between the p51 and RNase H domain (-Phe*Tyr-) within p66 of RT in the HIV-1 pol polyprotein. Processing by HIV proteinase (PR) in cis was monitored...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	FEBS letters 1991-06, Vol.283 (2), p.180-184
Hauptverfasser:	Jupp, Ray A., Phylip, Lowri H., Mills, John S., Le Grice, Stuart F.J., Kay, John
Format:	Artikel
Sprache:	eng
Schlagworte:	Base Sequence Biological and medical sciences Cleavage site mutagenesis Cloning, Molecular Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Gene Products, pol - genetics Gene Products, pol - metabolism Genetics HIV Protease - metabolism HIV-1 - genetics HIV-1 - metabolism HIV-1 proteinase Hydrolysis integrase. The nomenclature system of Schechter and Berger i.e. P2-P1P1′-P2′ is used to depict amino acids adjacent to the residues in the P1 and P1′ positions which contribute the scissile peptide bond (indicated by an asterisk) Microbiology Molecular Sequence Data Mutagenesis, Site-Directed Plasmids Polyprotein processing proteinase Recombinant Proteins - metabolism reverse transcriptase Specificity Substrate Specificity Virology
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!