Structure of a single-chain Fv fragment of an antibody that inhibits the HIV-1 and HIV-2 proteases

被引:2
|
作者
Lescar, J
Brynda, J
Fabry, M
Horejsi, M
Rezacova, P
Sedlacek, J
Bentley, GA
机构
[1] Inst Pasteur, Dept Biol Struct & Chim, Unite Immunol Struct, CNRS,URA 2185, F-75724 Paris 15, France
[2] European Synchrotron Radiat Facil, F-38043 Grenoble, France
[3] Acad Sci Czech Republ, Inst Mol Genet, Dept Gene Manipulat, CR-16637 Prague 6, Czech Republic
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2003年 / 59卷
关键词
D O I
10.1107/S0907444903003597
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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 Angstrom 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.
引用
收藏
页码:955 / 957
页数:3
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