(Q27703747)

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X-ray analysis of HIV-1 proteinase at 2.7 A resolution confirms structural homology among retroviral enzymes

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X-ray analysis of HIV-1 proteinase at 2.7 A resolution confirms structural homology among retroviral enzymes (English)

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John P. Overington

4

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2

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T Blundell

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Stephen P. Wood

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S Wood

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R Lapatto

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A Hemmings

3

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A Wilderspin

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J R Merson

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P J Whittle

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D E Danley

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K F Geoghegan

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16 November 1989

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342

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6247

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299-302

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Active human immunodeficiency virus protease is required for viral infectivity

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Structural evidence for gene duplication in the evolution of the acid proteases

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A structural model for the retroviral proteases.

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18th Sir Hans Krebs lecture. Knowledge-based protein modelling and design

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Crystal structure of a retroviral protease proves relationship to aspartic protease family

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Three-dimensional structure of aspartyl protease from human immunodeficiency virus HIV-1

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Retroviral proteinases. A second front against AIDS.

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Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 protease

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Structure and refinement of penicillopepsin at 1.8 Å resolution

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The active site of aspartic proteinases

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Three-dimensional structure of the complex of the Rhizopus chinensis carboxyl proteinase and pepstatin at 2.5-A resolution

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Conformational flexibility in the active sites of aspartyl proteinases revealed by a pepstatin fragment binding to penicillopepsin

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On the rational design of renin inhibitors: X-ray studies of aspartic proteinases complexed with transition-state analogues

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Molecular modeling of the HIV-1 protease and its substrate binding site

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Complete nucleotide sequence of the AIDS virus, HTLV-III

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A graphics model building and refinement system for macromolecules

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10.1038/342299A0

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