期刊
BIOCHEMISTRY
卷 40, 期 10, 页码 3167-3173出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi0019747
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资金
- NCI NIH HHS [P30 CA443703] Funding Source: Medline
- NHLBI NIH HHS [HL07653] Funding Source: Medline
- NIAMS NIH HHS [AR39750] Funding Source: Medline
S100 proteins are a family of 10-14 kDa EF-hand-containing calcium binding proteins that function to transmit calcium-dependent cell regulatory signals, S100 proteins have no intrinsic enzyme activity but bind in a calcium-dependent manner to target proteins to modulate target protein function, Transglutaminases are enzymes that catalyze the formation of covalent epsilon-(gamma -glutamyl)lysine bonds between protein-bound glutamine and lysine residues, In the present study we show that transglutaminase-dependent covalent modification is a property shared by several S100 proteins and that both type I and type II transglutaminases can modify S100 proteins. We further show that the reactive regions are at the solvent-exposed amino- and carboxyl-terminal ends of the protein, regions that specify S100 protein function. We suggest that transglutaminase-dependent modification is a general mechanism designed to regulate S100 protein function.
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