Structural studies of the retroviral proteinase from avian myeloblastosis associated virus.
The structure of the retroviral proteinase from avian myeloblastosis associated virus (MAV) has been determined and refined at 2.2 A resolution. This structure is compared with those of homologous proteinases from Rous sarcoma virus (RSV) and human immunodeficiency type 1 virus (HIV). Through comparison with the structure of a proteinase-inhibitor complex from HIV, a model of a complex between MAV proteinase and a peptide substrate has been generated. Examination of this model suggests structural basis for the diverse specifications of viral proteinases.
Ohlendorf
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DH
Du Pont Merck Pharmaceutical Company, Wilmington, Delaware 19880-0228.
Foundling
S I
SI
Wendoloski
J J
JJ
Sedlacek
J
J
Strop
P
P
Salemme
F R
FR
D000595:Amino Acid Sequence; D016282:Aspartic Acid Endopeptidases / Q000737:chemistry*; D009189:Avian Myeloblastosis Virus / Q000201:enzymology*; D001358:Avian Sarcoma Viruses / Q000201:enzymology; D046911:Macromolecular Substances; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity; D014764:Viral Proteins / Q000737:chemistry*
D046911:Macromolecular Substances; D014764:Viral Proteins; D016282:Aspartic Acid Endopeptidases