Crystal structure of a cross-reaction complex between an anti-HIV-1 protease antibody and an HIV-2 protease peptide
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
15721587
DOI
10.1016/j.jsb.2004.11.009
PII: S1047-8477(04)00224-2
Knihovny.cz E-resources
- MeSH
- Aspartic Acid Endopeptidases chemistry genetics immunology MeSH
- HIV Antibodies chemistry immunology MeSH
- HIV Protease immunology MeSH
- Protein Conformation MeSH
- Crystallography, X-Ray MeSH
- Humans MeSH
- Models, Molecular MeSH
- Molecular Sequence Data MeSH
- Antibodies, Monoclonal chemistry MeSH
- Peptides chemistry immunology MeSH
- Amino Acid Sequence MeSH
- Sequence Alignment MeSH
- Cross Reactions * MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Aspartic Acid Endopeptidases MeSH
- HIV Antibodies MeSH
- HIV Protease MeSH
- Antibodies, Monoclonal MeSH
- p16 protease, Human immunodeficiency virus 2 MeSH Browser
- Peptides MeSH
The monoclonal antibody 1696, elicited by HIV-1 protease, inhibits the activity of both HIV-1 and HIV-2 proteases with inhibition constants in the low nanomolar range. The antibody cross-reacts with peptides derived from the N-terminal region of both proteases. The crystal structure of the recombinant single-chain Fv fragment of 1696 complexed with an N-terminal peptide from the HIV-2 protease has been determined at 1.88A resolution. Interactions of the peptide with scFv1696 are compared with the previously reported structure of scFv1696 in complex with the corresponding peptide from HIV-1 protease. The origin of cross-reactivity of mAb1696 with HIV proteases is discussed.
References provided by Crossref.org
Optimization of the crystallizability of a single-chain antibody fragment
