| Autor: |
Wlodawer A; Macromolecular Structure Laboratory, NCI-Frederick Cancer Research and Development Center, Maryland 21702, USA., Gustchina A, Reshetnikova L, Lubkowski J, Zdanov A, Hui KY, Angleton EL, Farmerie WG, Goodenow MM, Bhatt D, et. al. |
| Jazyk: |
angličtina |
| Zdroj: |
Nature structural biology [Nat Struct Biol] 1995 Jun; Vol. 2 (6), pp. 480-8. |
| DOI: |
10.1038/nsb0695-480 |
| Abstrakt: |
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: |
MEDLINE |
| Externí odkaz: |
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