Crystal structure of a tethered dimer of HIV-1 proteinase complexed with an inhibitor
| Autor: | E.T. Baldwin, Y.-S. E. Cheng, Talapady N. Bhat, B. Liu, John W. Erickson |
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| Rok vydání: | 1994 |
| Předmět: |
Models
Molecular Protein Conformation Stereochemistry Dimer Molecular Sequence Data Crystallography X-Ray Biochemistry Structure-Activity Relationship chemistry.chemical_compound Protein structure HIV Protease Structural Biology Genetics Aspartic Acid Endopeptidases HIV Protease Inhibitor Structure–activity relationship Amino Acid Sequence Binding site Binding Sites Wild type Substrate (chemistry) HIV Protease Inhibitors Recombinant Proteins chemistry Alcohols Drug Design HIV-1 Linker Protein Binding |
| Zdroj: | Nature Structural Biology. 1:552-556 |
| ISSN: | 1072-8368 |
| DOI: | 10.1038/nsb0894-552 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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