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Preliminary crystallographic studies of an anti-HIV-1 protease antibody that inhibits enzyme activity
J Lescar, R Stouracova, MM Riottot, V Chitarra, J Brynda, M Fabry, M Horejsi, J Sedlacek, GA Bentley
Language English Country United States
Document type Research Support, Non-U.S. Gov't
Grant support
IZ3272
MZ0
CEP Register
Digital library NLK
Full text - Část
Source
NLK
Free Medical Journals
from 1992 to 1 year ago
PubMed Central
from 1992 to 1 year ago
Europe PubMed Central
from 1992 to 1 year ago
Wiley Free Content
from 1996 to 1 year ago
PubMed
8732768
Knihovny.cz E-resources
- MeSH
- HIV Antigens * immunology MeSH
- HIV Antibodies * pharmacology chemistry immunology MeSH
- HIV-1 * enzymology immunology MeSH
- HIV Protease * immunology MeSH
- Immunoglobulin Fab Fragments chemistry immunology MeSH
- HIV Protease Inhibitors * chemistry immunology MeSH
- Crystallography, X-Ray MeSH
- Antibodies, Monoclonal * pharmacology chemistry immunology MeSH
- Mice, Inbred BALB C MeSH
- Mice MeSH
- Peptide Fragments immunology MeSH
- Recombinant Fusion Proteins immunology MeSH
- Cross Reactions MeSH
- Animals MeSH
- Check Tag
- Mice MeSH
- Animals MeSH
- Publication type
- Research Support, Non-U.S. Gov't MeSH
F11.2.32, a monoclonal antibody directed against the HIV-1 protease, displays strong inhibitory effects toward the catalytic activity of the enzyme. The antibody cross-reacts with peptides 36-46 and 36-57 from the protease. Crystals of the Fab have been obtained both in the free state and as complexes formed with the protease peptide fragments, 36-46 and 36-57. Diffraction data have been collected for the free and complexed forms of Fab F11.2.32 and preliminary models for the crystal structures were obtained by molecular replacement.
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