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Biochemistry. 1987 Nov 17;26(23):7466-70.

Amino acid sequence of P-57, a neurospecific calmodulin-binding protein.

Author information

1
Department of Biochemistry, University of Washington, Seattle 98195.

Abstract

The amino acid sequence was determined for bovine brain P-57, a neurospecific, membrane-associated, calmodulin-binding protein. It consists of a single 239-residue polypeptide chain blocked at its amino terminus and containing an unusually hydrophilic amino acid composition. Seventy percent of the molecule is composed of Glu/Gln, Ala, Lys, Asp/Asn, and Pro; there is only one aromatic residue. A lack of favorable cleavage sites required that a particularly wide variety of digests and subdigests be performed to obtain appropriate sets of overlapping peptides. This protein is clearly homologous with the cDNA-derived sequence of mouse brain P-57, although the bovine protein is 12 amino acid residues longer; the homology is less obvious in the middle sections of the two sequences. Bovine brain P-57 lacks homology with any other protein in an updated sequence database. A segment reported to interact with calmodulin (Arg-Gly-His-Ile-Thr-Arg-Lys-Lys-Leu) is placed at residues 43-51 within the only extended segment of P-57 that carries the net positive charge that would favor that interaction. There is no hydrophobic segment characteristic of many proteins that interact with membranes.

PMID:
2962637
DOI:
10.1021/bi00397a040
[Indexed for MEDLINE]

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