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• W2023753758 endingPage "725" @default.
• W2023753758 startingPage "719" @default.
• W2023753758 abstract "Abstract The annexin family of proteins is characterized by a conserved core domain that binds to phospholipids in a Ca-dependent manner. Each annexin also has a structurally distinct N-terminal domain that may impart functional specificity. To search for cellular proteins that interact with the N-terminal domain of annexin I, we constructed a fusion protein consisting of glutathione S-transferase fused to amino acids 2-47 of human annexin I (GST-AINT; AINT = annexin I N-terminal). Extracts from metabolically labeled A431 cells contained a single protein (M 10,000) that bound to GST-AINT in a Ca-dependent manner. A synthetic peptide corresponding to amino acids 2-18 of annexin I inhibited the binding of the 10-kDa protein to GST-AINT with half-maximal inhibition occurring at 15 μM peptide. In cellular extracts, endogenous annexin I and the 10-kDa protein associated in a reversible Ca-dependent manner. Experiments with other annexins and with N-terminal truncated forms of annexin I indicated that the 10-kDa protein bound specifically to a site within the first 12 amino acids of annexin I. The 10-kDa protein was purified from human placenta by hydrophobic and affinity chromatography. Amino acid sequence analysis indicated that the 10-kDa protein is the human homologue of S100C, a recently identified member of the S100 subfamily of EF-hand Ca-binding proteins." @default.
• W2023753758 created "2016-06-24" @default.
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• W2023753758 date "1996-01-01" @default.
• W2023753758 modified "2023-10-13" @default.
• W2023753758 title "Calcium-dependent Binding of S100C to the N-terminal Domain of Annexin I" @default.
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• W2023753758 doi "https://doi.org/10.1074/jbc.271.2.719" @default.
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