title: Structural studies of the retroviral proteinase from avian myeloblastosis associated virus.
abstract: 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.
authors.affiliation: Du Pont Merck Pharmaceutical Company, Wilmington, Delaware 19880-0228.
authors.forename: D H
authors.initials: DH
authors.lastname: Ohlendorf
authors.forename: S I
authors.initials: SI
authors.lastname: Foundling
authors.forename: J J
authors.initials: JJ
authors.lastname: Wendoloski
authors.forename: J
authors.initials: J
authors.lastname: Sedlacek
authors.forename: P
authors.initials: P
authors.lastname: Strop
authors.forename: F R
authors.initials: FR
authors.lastname: Salemme
mesh_terms: 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*
chemical_list: D046911:Macromolecular Substances; D014764:Viral Proteins; D016282:Aspartic Acid Endopeptidases