Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystal structure of a tethered dimer of HIV-1 proteinase complexed with an inhibitor.,Bhat TN, Baldwin ET, Liu B, Cheng YS, Erickson JW Nat Struct Biol. 1994 Aug;1(8):552-6. PMID:7664084[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bhat TN, Baldwin ET, Liu B, Cheng YS, Erickson JW. Crystal structure of a tethered dimer of HIV-1 proteinase complexed with an inhibitor. Nat Struct Biol. 1994 Aug;1(8):552-6. PMID:7664084
