Lescar Julien, Brynda Jiri, Fabry Milan, Horejsi Magda, Rezacova Pavlina, Sedlacek Juraj, Bentley Graham A
European Synchrotron Radiation Facility, BP 220, F-38043 Grenoble, France.
Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):955-7. doi: 10.1107/s0907444903003597. Epub 2003 Apr 25.
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.