We report here two crystal structures of a recombinant single-chain Fv fragment of mAb 1696,expressed in E. coli, as a complex with a cross-reactive peptides from the HIV-1 PR and theHIV-2 PR at 2.7 ? resolution and 1.9 ? resolution respectively. On the basis of the interactionsseen in the complex three-dimensional structures, the cross-reactivity between mAb 1696 withthe HIV-1 and HIV-2 protease and their N-terminal peptides can be explained. In addition, acandidate mechanism of HIV PR inhibition by mAb 1696 is proposed which may help thedesign of alternative HIV protease inhibitors, aimed at dissociating the homodimeric viral enzyme."> We report here two crystal structures of a recombinant single-chain Fv fragment of mAb 1696,expressed in E. coli, as a complex with a cross-reactive peptides from the HIV-1 PR and theHIV-2 PR at 2.7 ? resolution and 1.9 ? resolution respectively. On the basis of the interactionsseen in the complex three-dimensional structures, the cross-reactivity between mAb 1696 withthe HIV-1 and HIV-2 protease and their N-terminal peptides can be explained. In addition, acandidate mechanism of HIV PR inhibition by mAb 1696 is proposed which may help thedesign of alternative HIV protease inhibitors, aimed at dissociating the homodimeric viral enzyme."> We report here two crystal structures of a recombinant single-chain Fv fragment of mAb 1696,expressed in E. coli, as a complex with a cross-reactive peptides from the HIV-1 PR and theHIV-2 PR at 2.7 ? resolution and 1.9 ? resolution respectively. On the basis of the interactionsseen in the complex three-dimensional structures, the cross-reactivity between mAb 1696 withthe HIV-1 and HIV-2 protease and their N-terminal peptides can be explained. In addition, acandidate mechanism of HIV PR inhibition by mAb 1696 is proposed which may help thedesign of alternative HIV protease inhibitors, aimed at dissociating the homodimeric viral enzyme."> Structural basis of HIV-1 and HIV-2 protease inhibition bya monoclona…
Number of the records: 1  

Structural basis of HIV-1 and HIV-2 protease inhibition bya monoclonal antibody

    1.
    Řezáčová, Pavlína - Lescar, J. - Brynda, Jiří - Fábry, Milan - Bentley, G. A. - Sedláček, Juraj
    Structural basis of HIV-1 and HIV-2 protease inhibition bya monoclonal antibody.
    Material Structure in Chemistry, Biology, Physics and Technology. Praha, Česká republika: Czech and Slovak Crystallographic Association, 2003 - (Kužel, R.; Hašek, J.; Fiala, J.; Wiss, Z.), s. 70. ISSN 1211-5894.
    [Meetingof the Czech and Slovak structural biologist /2./. Nové Hrady (CZ), 13.03.2003-15.03.2003]
    http://hdl.handle.net/11104/0087286

Number of the records: 1  

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