Structural highlights
Function
KV2A7_MOUSE
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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
