Substrates and inhibitors of human T-cell leukemia virus type 1 (HTLV-1) proteinase.
Human T-cell leukemia virus type 1 (HTLV-1) proteinase, a 125 residue polypeptide, was chemically synthesized using the solid phase method. The crude product was purified, renaturated and proteolytic activity was tested using oligopeptide substrates derived from processing sites of various retroviral polyproteins. Cleavage of the oligopeptide substrates together with an initial study using a series of HIV-1 and MAV (myeloblastosis associated virus) proteinase inhibitors suggest that the substrate specificity of HTLV-1 proteinase is very close to that of BLV (bovine leukemia virus) proteinase and distinct from that of both HIV-1 and MAV proteinases.
Hrusková-Heidingsfeldová
O
O
Czech Academy of Sciences, Institute of Organic Chemistry and Biochemistry, Prague, Czech Republic.
Bláha
I
I
Urban
J
J
Strop
P
P
Pichová
I
I
D000595:Amino Acid Sequence; D016282:Aspartic Acid Endopeptidases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D015368:Human T-lymphotropic virus 1 / Q000201:enzymology*; D006801:Humans; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis / Q000378:metabolism* / Q000494:pharmacology*; D011480:Protease Inhibitors / Q000138:chemical synthesis / Q000494:pharmacology*; D017510:Protein Folding; D013379:Substrate Specificity
D009842:Oligopeptides; D011480:Protease Inhibitors; D016282:Aspartic Acid Endopeptidases; C079711:HTLV-1 protease