NDLI: Identification and characterization of the calmodulin-binding domain of neuromodulin, a neurospecific calmodulin-binding protein.

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Identification and characterization of the calmodulin-binding domain of neuromodulin, a neurospecific calmodulin-binding protein.

Content Provider	Semantic Scholar
Author	Alexander, Kenneth Wakim, Bassam T. Doyle, Gerald S. Walsh, Kenneth A. Storm, Daniel R.
Copyright Year	1988
Abstract	Neuromodulin (formerly designated P-57) is an abundant, neural specific, calmodulin-binding protein which exhibits higher affinity for calmodulin in the absence of free Ca2+ than in the presence of free Ca2+. In this study a series of proteolytic fragments of neuromodulin were systematically screened for calmodulin-Sepharose binding activity. A 9-amino acid fragment, designated M1-C1 and having the sequence RGHITRKKL, was identified as the putative CaM-binding domain of neuromodulin. Two heptadecapeptides, designated FP57-Phe and FP57-Trp, were synthesized, each containing the M1-C1 sequence and the four flanking amino acids from each site. The FP57-Trp peptide contained a tryptophan residue in place of the native phenylalanine. Anti-FP57-Phe antibody binding to neuromodulin was inhibited by preincubation of antibodies with excess FP57-Phe. 125I-CaM gel overlay of neuromodulin was inhibited by anti-FP57-Phe antibodies. Addition of CaM to FP57-Trp increased peptide tryptophanyl fluorescence. In the presence of Ca2+, the stoichiometry of the FP57-Trp.CaM complex was 1:1, FP57-Trp binding to CaM was competitive with neuromodulin. The Ca2+-independent dissociation constant of the FP57-Phe.CaM complex was 0.41 microM. The Ca2+-dependent affinity of the complex could not be measured directly but appeared to be significantly greater than the Ca2+-independent affinity.
File Format	PDF HTM / HTML
PubMed reference number	2967288
Journal	Medline
Volume Number	263
Issue Number	16
Alternate Webpage(s)	http://www.jbc.org/content/263/16/7544.full.pdf
Journal	The Journal of biological chemistry
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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