Title : Cysteine oxidation in the mitogenic S100B protein leads to changes in phosphorylation by catalytic CKII-alpha subunit.

Pub. Date : 1998 Feb 13

PMID : 9461574






5 Functional Relationships(s)
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1 Cysteine oxidation in the mitogenic S100B protein leads to changes in phosphorylation by catalytic CKII-alpha subunit. Cysteine S100 calcium binding protein B Homo sapiens
2 The extracellular S100B activities rely on the oxidation of the protein cysteine residues (Kligman, D., and Marshak, D. R. (1985) Proc. Cysteine S100 calcium binding protein B Homo sapiens
3 Here we show that oxidation of the S100B cysteine residues, Cys-68 and Cys-84, induces a conformational change in the protein structure, unmasking a canonical CKII phosphorylation site located within the typical EF-hand calcium-binding site IIbeta. Cysteine S100 calcium binding protein B Homo sapiens
4 Here we show that oxidation of the S100B cysteine residues, Cys-68 and Cys-84, induces a conformational change in the protein structure, unmasking a canonical CKII phosphorylation site located within the typical EF-hand calcium-binding site IIbeta. Cysteine S100 calcium binding protein B Homo sapiens
5 Here we show that oxidation of the S100B cysteine residues, Cys-68 and Cys-84, induces a conformational change in the protein structure, unmasking a canonical CKII phosphorylation site located within the typical EF-hand calcium-binding site IIbeta. Cysteine S100 calcium binding protein B Homo sapiens