title: Caldesmon structure and function: sequence analysis of a 35 kilodalton actin- and calmodulin-binding fragment from the C-terminus of the turkey gizzard protein.
abstract: We have determined the amino acid sequence of a 35 kDa proteolytic fragment ("CaD35") derived from the C-terminus of turkey gizzard caldesmon. This 239-residue peptide contains binding sites for actin and calmodulin. Residues 1-96 of CaD35 comprise "CaD15", an actin-binding subfragment which we previously showed to resemble the tropomyosin-binding segment of troponin T. The remainder of the CaD35 sequence shows no significant similarity to other proteins. Residues 111-128 may form a basic, amphipathic helix which interacts with calmodulin.
authors.affiliation: Department of Biological Chemistry, School of Medicine, University of Maryland, Baltimore 21201.
authors.forename: J
authors.initials: J
authors.lastname: Leszyk
authors.forename: D
authors.initials: D
authors.lastname: Mornet
authors.forename: E
authors.initials: E
authors.lastname: Audemard
authors.forename: J H
authors.initials: JH
authors.lastname: Collins
mesh_terms: D000199:Actins / Q000378:metabolism; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D002147:Calmodulin / Q000378:metabolism; D002148:Calmodulin-Binding Proteins; D002851:Chromatography, High Pressure Liquid; D003488:Cyanogen Bromide; D005895:Gizzard, Avian / Q000032:analysis*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments; D010766:Phosphorylation; D011487:Protein Conformation; D012697:Serine Endopeptidases; D014335:Tropomyosin / Q000378:metabolism; D014357:Trypsin; D014422:Turkeys
chemical_list: D000199:Actins; D000596:Amino Acids; D002147:Calmodulin; D002148:Calmodulin-Binding Proteins; D010446:Peptide Fragments; D014335:Tropomyosin; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase; D014357:Trypsin; D003488:Cyanogen Bromide