title: Importance of the C-terminal part of actin in interactions with calponin.
abstract: Native, modified or trypsin-truncated actin was used to study the impact of modifying the C-terminal part of actin (the last three amino acids) on interactions with calponin. We used three different techniques to show that these amino acids are essential for the actin-calponin interface. The locations of actin-calponin interaction sites on the actin crystal are discussed in terms of previously reported data.
authors: INSERM U300, Faculté de Pharmacie, Montpellier, France.
authors: A
authors: A
authors: Bonet-Kerrache
authors: D
authors: D
authors: Mornet
mesh_terms: D000199:Actins / Q000737:chemistry* / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D002135:Calcium-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D002645:Chickens; D004797:Enzyme-Linked Immunosorbent Assay; D005895:Gizzard, Avian; D007700:Kinetics; D008840:Microfilament Proteins; D018482:Muscle, Skeletal; D009130:Muscle, Smooth; D010446:Peptide Fragments / Q000737:chemistry* / Q000378:metabolism; D017433:Protein Structure, Secondary; D011817:Rabbits; D014357:Trypsin; D000096985:Calponins
chemical_list: D000199:Actins; D002135:Calcium-Binding Proteins; D008840:Microfilament Proteins; D010446:Peptide Fragments; D014357:Trypsin; D000096985:Calponins