Three-dimensional structure of aspartyl protease from human immunodeficiency virus HIV-1 |
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| Authors: | M A Navia P M Fitzgerald B M McKeever C T Leu J C Heimbach W K Herber I S Sigal P L Darke J P Springer |
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| Affiliation: | Department of Biophysical Chemistry, Merck Sharp and Dohme Research Laboratories, Rahway, New Jersey 07065. |
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| Abstract: | The 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. |
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