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, which was raised against the HIV-1 protease, inhibits the catalytic activity of the enzyme from both the HIV-1 and HIV-2 strains. The antibody cross-reacts with peptides containing the N-terminus of the enzyme, which is highly conserved between these strains. The crystal structure of a single-chain Fv fragment of 1696 (scFv-1696) in the non-complexed form, solved at 1.7 A resolution, is compared with the previously reported non-complexed Fab-1696 and antigen-bound scFv-1696 structures. Large conformational changes in the third hypervariable region of the heavy chain and differences in relative orientation of the variable domains are observed between the different structures.
Structure of a single-chain Fv fragment of an antibody that inhibits the HIV-1 and HIV-2 proteases.,Lescar J, Brynda J, Fabry M, Horejsi M, Rezacova P, Sedlacek J, Bentley GA Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):955-7. Epub 2003, Apr 25. PMID:12777823[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lescar J, Brynda J, Fabry M, Horejsi M, Rezacova P, Sedlacek J, Bentley GA. Structure of a single-chain Fv fragment of an antibody that inhibits the HIV-1 and HIV-2 proteases. Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):955-7. Epub 2003, Apr 25. PMID:12777823
