2hvp | pdb_00002hvp
From Proteopedia
THREE-DIMENSIONAL STRUCTURE OF ASPARTYL PROTEASE FROM HUMAN IMMUNODEFICIENCY VIRUS HIV-1
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Structural highlights
Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of the protease of the human immunodeficiency virus type (HIV-1), which releases structural proteins and enzymes from viral polyprotein products, has been determined to 3 A resolution. Large regions of the protease dimer, including the active site, have structural homology to the family of microbial aspartyl proteases. The structure suggests a mechanism for the autoproteolytic release of protease and a role in the control of virus maturation. Three-dimensional structure of aspartyl protease from human immunodeficiency virus HIV-1.,Navia MA, Fitzgerald PM, McKeever BM, Leu CT, Heimbach JC, Herber WK, Sigal IS, Darke PL, Springer JP Nature. 1989 Feb 16;337(6208):615-20. PMID:2645523[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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