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Cysteine-rich zinc finger motifs

The interaction of DAG with PKC is best illustrated with the model for cPKC activation. DAG and DAG-mimicking phorbol esters such as phorbol-12-myristate-13-acetate (PMA) bind cPKC at the cysteine-rich Cl domain within the amino terminus. The Cl domain consists of two highly conserved zinc-finger motifs (Cla and Clb) that are arranged in tandem. Each motif is composed of 50-51 amino acids with the sequence H-Xj C-X C-Xu j C-X C-X H-X C-X C, where H represents histidine and C represents cysteine. In vitro studies suggest that there are two functional consequences of DAG binding to cPKC ... [Pg.47]

CxxCG Zn finger Protein kinase C, AdK, HIV NCP, raR This motif is found in zinc-containing small, cysteine-rich domains and it is central to their core structure. [Pg.119]

See other pages where Cysteine-rich zinc finger motifs is mentioned: [Pg.894]    [Pg.239]    [Pg.894]    [Pg.1949]    [Pg.203]    [Pg.894]    [Pg.239]    [Pg.894]    [Pg.1949]    [Pg.203]    [Pg.159]    [Pg.210]    [Pg.227]    [Pg.5120]    [Pg.5119]    [Pg.164]    [Pg.343]    [Pg.414]    [Pg.431]    [Pg.5542]    [Pg.149]    [Pg.5541]    [Pg.336]   
See also in sourсe #XX -- [ Pg.203 ]



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