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• W2083578765 startingPage "1376" @default.
• W2083578765 abstract "To obtain site-specific information about individual EF-hand motifs, the EF-hand Ca(2+)-binding loops from site III and site IV of calmodulin (CaM) were inserted separately into a non-Ca(2+)-binding cell adhesion protein, domain 1 of CD2 (denoted as CaM-CD2-III-5G-52 and CaM-CD2-IV-5G-52). Structural analyses using various spectroscopic methods have shown that the host protein CD2 retains its native structure after the insertion of the 12-residue loops. The Tb(3+) fluorescence enhancement upon formation of a Tb(3+)-protein complex and the direct competition by La(3+) and Ca(2+) suggest that native Ca(2+)-binding pockets are formed in both engineered proteins. Moreover, as revealed by NMR, both Ca(2+) and La(3+) specifically interact with the residues at the grafted EF-loop. The CaM-CD2-III-5G-52 has stronger affinities to Ca(2+), Tb(3+) and La(3+) than CaM-CD2-IV-5G-52, indicating differential intrinsic metal-binding affinities of the EF-loops." @default.
• W2083578765 created "2016-06-24" @default.
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• W2083578765 date "2005-06-01" @default.
• W2083578765 modified "2023-09-30" @default.
• W2083578765 title "Calcium and lanthanide affinity of the EF-loops from the C-terminal domain of calmodulin" @default.
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• W2083578765 doi "https://doi.org/10.1016/j.jinorgbio.2005.03.011" @default.
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