Structure of an inhibitor complex of the proteinase from feline immunodeficiency virus
| Autor: | Alexander Wlodawer, Alla Gustchina, Ludmila Reshetnikova, Jacek Lubkowski, Alexander Zdanov, Kwan Y. Hui, Eddie L. Angleton, William G. Farmerie, Maureen M. Goodenow, Deepa Bhatt, Li Zhang, Ben M. Dunn |
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| Rok vydání: | 1995 |
| Předmět: |
Models
Molecular Feline immunodeficiency virus Protein Conformation Peptidomimetic animal diseases viruses Molecular Sequence Data Statistics as Topic Sequence alignment Immunodeficiency Virus Feline Biology Cleavage (embryo) Substrate Specificity law.invention Viral Proteins Protein structure HIV Protease X-Ray Diffraction Structural Biology law Endopeptidases Aspartic Acid Endopeptidases Protease Inhibitors Amino Acid Sequence Amino Acids Molecular Biology Peptide sequence chemistry.chemical_classification Binding Sites Molecular Structure virus diseases biology.organism_classification Virology Kinetics Enzyme chemistry Recombinant DNA Peptides Oligopeptides Sequence Alignment |
| Zdroj: | Nature Structural & Molecular Biology. 2:480-488 |
| ISSN: | 1545-9985 1545-9993 |
| DOI: | 10.1038/nsb0695-480 |
| Popis: | The crystal structure of a recombinant form of the proteinase encoded by the feline immunodeficiency virus (FIV PR) has been solved at 2 A resolution and refined to an R-factor of 0.148. The refined structure includes a peptidomimetic, statine-based inhibitor, LP-149, which is an even more potent inhibitor of HIV PR. Kinetic parameters were obtained for the cleavage of five substrates by FIV PR, and inhibition constants were measured for four inhibitors. The structure of FIV PR resembles other related retroviral enzymes although few inhibitors of HIV PR are capable of inhibiting FIV PR. The structure of FIV PR will enhance our knowledge of this class of enzymes, and will direct testing of new proteinase inhibitors in a feline animal model. |
| Databáze: | OpenAIRE |
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