Structural highlights
Function
[GAG_AVIMA] Specifically liberates the five major structural proteins from the common gag precursor, as well as reverse transcriptase and integrase from the gag-pol precursor.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structural studies of the retroviral proteinase from avian myeloblastosis associated virus.,Ohlendorf DH, Foundling SI, Wendoloski JJ, Sedlacek J, Strop P, Salemme FR Proteins. 1992 Nov;14(3):382-91. PMID:1332025[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ohlendorf DH, Foundling SI, Wendoloski JJ, Sedlacek J, Strop P, Salemme FR. Structural studies of the retroviral proteinase from avian myeloblastosis associated virus. Proteins. 1992 Nov;14(3):382-91. PMID:1332025 doi:http://dx.doi.org/10.1002/prot.340140307
