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.
    SYSNO ASEP0191543
    Document TypeK - Proceedings Paper (Czech conf.)
    R&D Document TypeConference Paper
    TitleStructural basis of HIV-1 and HIV-2 protease inhibition bya monoclonal antibody
    Author(s) Řezáčová, Pavlína (UMG-J) RID
    Lescar, J. (FR)
    Brynda, Jiří (UMG-J) RID
    Fábry, Milan (UMG-J) RID
    Bentley, G. A. (FR)
    Sedláček, Juraj (UMG-J) RID
    Source TitleMaterial Structure in Chemistry, Biology, Physics and Technology. - Praha, Česká republika : Czech and Slovak Crystallographic Association, 2003 / Kužel R. ; Hašek J. ; Fiala J. ; Wiss Z. - ISSN 1211-5894
    s. 70
    Number of pages2 s.
    ActionMeetingof the Czech and Slovak structural biologist /2./
    Event date13.03.2003-15.03.2003
    VEvent locationNové Hrady
    CountryCZ - Czech Republic
    Event typeCST
    Languageeng - English
    CountryCZ - Czech Republic
    Keywordsantibody fragment ; crystal structure ; HIV protease inhibition
    Subject RIVCE - Biochemistry
    R&D ProjectsGV203/98/K023 GA ČR - Czech Science Foundation (CSF)
    CEZAV0Z5052915 - UMG-J
    AnnotationThe 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.
    WorkplaceInstitute of Molecular Genetics
    ContactNikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217
    Year of Publishing2004

Number of the records: 1  

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