Open AccessLocalization of a vitamin‐D‐binding protein interaction site in the COOH‐terminal sequence of actin
Author(s) -
HOUMEIDA Ahmed,
HANIN Veronique,
CONSTANS Jacques,
BENYAMIN Yves,
ROUSTAN Claude
Publication year - 1992
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1992.tb16575.x
Subject(s) - actin , actin binding protein , vitamin d binding protein , sequence (biology) , binding site , actina , plasma protein binding , vitamin , monomer , chemistry , binding protein , peptide sequence , terminal (telecommunication) , microbiology and biotechnology , biochemistry , biology , actin cytoskeleton , gene , cytoskeleton , computer science , cell , polymer , organic chemistry , telecommunications
The serum vitamin D binding protein is the carrier of vitamin D and its derivatives in the plasma. One of the known roles of this protein is to sequester monomeric actin in the blood, therefore implicating this protein in actin elimination. However, its binding site at the surface of actin is poorly delimited. We report here the results of a study which locates, using several actin fragments together with immunological probes, a vitamin D binding protein site near the COOH‐terminal extremity. Thus, the interface is delimited by the sequence 360–372 in subdomain I of actin.