1MVP

STRUCTURAL STUDIES OF THE RETROVIRAL PROTEINASE FROM AVIAN MYELOBLASTOSIS ASSOCIATED VIRUS

Summary for 1MVP

• Entry DOI: 10.2210/pdb1mvp/pdb
• Descriptor: MYELOBLASTOSIS ASSOCIATED VIRAL PROTEASE (2 entities in total)
• Functional Keywords: hydrolase(aspartic proteinase)
• Biological source: Avian myeloblastosis-associated virus
• Total number of polymer chains: 2
• Total formula weight: 27223.67

Authors

Ohlendorf, D.H.,Foundling, S.I.,Salemme, F.R. (deposition date: 1990-09-07, release date: 1992-01-15, Last modification date: 2024-02-14)

Primary citation

Ohlendorf, D.H.,Foundling, S.I.,Wendoloski, J.J.,Sedlacek, J.,Strop, P.,Salemme, F.R.
Structural studies of the retroviral proteinase from avian myeloblastosis associated virus.
Proteins, 14:382-391, 1992

PubMed 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.

PubMed: 1332025
DOI: 10.1002/prot.340140307

Experimental method

X-RAY DIFFRACTION (2.2 Å)