title: Interaction of the 47-kDa talin fragment and the 32-kDa vinculin fragment with acidic phospholipids: a computer analysis.
abstract: In recent in vitro experiments, it has been demonstrated that the 47-kDa fragment of the talin molecule and the 32-kDa fragment of the vinculin molecule interact with acidic phospholipids. By using a computer analysis method, we determined the hydrophobic and amphipathic stretches of these fragments and, by applying a purpose-written matrix method, we ascertained the molecular amphipathic structure of alpha-helices. Calculations for the 47-kDa mouse talin fragment (residues 1-433; NH2-terminal region) suggest specific interactions of residues 21-39, 287-342, and 385-406 with acidic phospholipids and a general lipid-binding domain for mouse talin (primary amino acid sequence 385-401) and for Dictyostelium talin (primary amino acid sequence 348-364). Calculations for the 32-kDa chicken embryo vinculin fragment (residues 858-1066; COOH-terminal region) and from nematode vinculin alignment indicate for chicken embryo vinculin residues 935-978 and 1020-1040 interactions with acidic phospholipids. Experimental confirmation has been given for vinculin (residues 916-970), and future detailed experimental analyses are now needed to support the remaining computational data.
authors.affiliation: Department of Biophysics, Technical University of Munich, Garching, Germany.
authors.forename: M
authors.initials: M
authors.lastname: Tempel
authors.forename: W H
authors.initials: WH
authors.lastname: Goldmann
authors.forename: G
authors.initials: G
authors.lastname: Isenberg
authors.forename: E
authors.initials: E
authors.lastname: Sackmann
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002645:Chickens; D051379:Mice; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009348:Nematoda; D010446:Peptide Fragments / Q000737:chemistry* / Q000378:metabolism; D010743:Phospholipids / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid; D012984:Software; D016608:Talin / Q000737:chemistry* / Q000378:metabolism; D016596:Vinculin / Q000737:chemistry* / Q000378:metabolism
chemical_list: D010446:Peptide Fragments; D010743:Phospholipids; D016608:Talin; D016596:Vinculin