1HVC

CRYSTAL STRUCTURE OF A TETHERED DIMER OF HIV-1 PROTEASE COMPLEXED WITH AN INHIBITOR

Summary for 1HVC

• Entry DOI: 10.2210/pdb1hvc/pdb
• Descriptor: HIV-1 PROTEASE, N-{1-BENZYL-(2S,3S)-2,3-DIHYDROXY-4-[3-METHYL-2-(3-METHYL-3-PYRIDIN-2-YLMETHYL-UREIDO)-BUTYRYLAMINO]-5-PHENYL-PENTYL}-3-METHYL-2-(3-METHYL-3-PYRIDIN-2-YLMETHYL-UREIDO)-BUTYRAMIDE (3 entities in total)
• Functional Keywords: hydrolase(acid protease)
• Biological source: Human immunodeficiency virus 1
• Total number of polymer chains: 1
• Total formula weight: 22756.83

Authors

Bhat, T.N.,Baldwin, E.T.,Erickson, J.W. (deposition date: 1994-06-22, release date: 1994-10-15, Last modification date: 2024-02-07)

Primary citation

Bhat, T.N.,Baldwin, E.T.,Liu, B.,Cheng, Y.S.,Erickson, J.W.
Crystal structure of a tethered dimer of HIV-1 proteinase complexed with an inhibitor.
Nat.Struct.Biol., 1:552-556, 1994

PubMed Abstract: HIV-1 proteinase (HIV PR) is a dimeric enzyme composed of two identical polypeptide chains that associate with twofold symmetry. We have determined to 1.8 A the crystal structure of a covalently tethered dimer of HIV PR. The tethered dimer:inhibitor complex is identical in nearly every respect to the complex of the same inhibitor with the wild type dimeric molecule, except for the linker region. Our results suggest that the tethered dimer may be a useful surrogate enzyme for studying the effects of single site mutations on substrate and inhibitor binding as well as on enzyme asymmetry, and for simulating independent mutational drift of the two domains which has been proposed to have led to the evolution of modern day, single-chain aspartic proteinases.

PubMed: 7664084
DOI: 10.1038/nsb0894-552

Experimental method

X-RAY DIFFRACTION (1.8 Å)