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2j9j
From Proteopedia
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[[Category: rna-directed dna polymerase]] | [[Category: rna-directed dna polymerase]] | ||
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Revision as of 15:23, 30 October 2007
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ATOMIC-RESOLUTION CRYSTAL STRUCTURE OF CHEMICALLY-SYNTHESIZED HIV-1 PROTEASE COMPLEXED WITH INHIBITOR JG-365
Overview
The human immunodeficiency virus 1 (HIV-1) protease (PR) is an aspartyl, protease essential for HIV-1 viral infectivity. HIV-1 PR has one catalytic, site formed by the homodimeric enzyme. We chemically synthesized fully, active HIV-1 PR using modern ligation methods. When complexed with the, classic substrate-derived inhibitors JG-365 and MVT-101, the synthetic, HIV-1 PR formed crystals that diffracted to 1.04- and 1.2-A resolution, respectively. These atomic-resolution structures revealed additional, structural details of the HIV-1 PR's interactions with its active site, ligands. Heptapeptide inhibitor JG-365, which has a hydroxyethylamine, moiety in place of the scissile bond, binds in two equivalent antiparallel, orientations within the catalytic groove, whereas the reduced isostere, ... [(full description)]
About this Structure
2J9J is a [Protein complex] structure of sequences from [Human immunodeficiency virus 1] with SO4, ACT and GOL as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Insights from Atomic-Resolution X-Ray Structures of Chemically Synthesized HIV-1 Protease in Complex with Inhibitors., Johnson EC, Malito E, Shen Y, Pentelute B, Rich D, Florian J, Tang WJ, Kent SB, J Mol Biol. 2007 Oct 26;373(3):573-86. Epub 2007 Aug 2. PMID:17869270
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