Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
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.
Crystal structure of a cross-reaction complex between an anti-HIV-1 protease antibody and an HIV-2 protease peptide.,Rezacova P, Brynda J, Lescar J, Fabry M, Horejsi M, Sieglova I, Sedlacek J, Bentley GA J Struct Biol. 2005 Mar;149(3):332-7. PMID:15721587[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Rezacova P, Brynda J, Lescar J, Fabry M, Horejsi M, Sieglova I, Sedlacek J, Bentley GA. Crystal structure of a cross-reaction complex between an anti-HIV-1 protease antibody and an HIV-2 protease peptide. J Struct Biol. 2005 Mar;149(3):332-7. PMID:15721587 doi:10.1016/j.jsb.2004.11.009
