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.
    SYSNO0191543
    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. s. 70. - Praha, Česká republika : Czech and Slovak Crystallographic Association, 2003 / Kužel R. ; Hašek J. ; Fiala J. ; Wiss Z.
    Conference Meetingof the Czech and Slovak structural biologist /2./, Nové Hrady, 13.03.2003-15.03.2003
    Document TypeKonferenční příspěvek (tuzemská konf.)
    Grant GV203/98/K023 GA ČR - Czech Science Foundation (CSF)
    CEZAV0Z5052915 - UMG-J
    Languageeng
    CountryCZ
    Keywords antibody fragment * crystal structure * HIV protease inhibition
    Permanent Linkhttp://hdl.handle.net/11104/0087286
     

Number of the records: 1  

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