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

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    0191543 - UMG-J 20033037 RIV CZ eng K - Conference Paper (Czech conference)
    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]
    R&D Projects: GA ČR GV203/98/K023
    Institutional research plan: CEZ:AV0Z5052915
    Keywords : antibody fragment * crystal structure * HIV protease inhibition
    Subject RIV: CE - Biochemistry

    The murine monoclonal antibody 1696, produced by immunisation with the HIV-1 protease,inhibits the catalytic activity of the enzyme of both the HIV-1 and HIV-2 isolates, with inhibitionconstants in the low nanomolar range. This antibody cross-reacts with peptides that include theN-terminus of the enzyme (residues 1-7), a region which is highly conserved in sequence amongdifferent viral strains and which, furthermore, is crucial for homodimerization to the activeenzymatic form.<?xml:namespace prefix = o ns = "urn:schemas-microsoft-com:office:office" />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.
    Permanent Link: http://hdl.handle.net/11104/0087286

     
     

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