M. Tempel et al., INTERACTION OF THE 47-KDA TALIN FRAGMENT AND THE 32-KDA VINCULIN FRAGMENT WITH ACIDIC PHOSPHOLIPIDS - A COMPUTER-ANALYSIS, Biophysical journal, 69(1), 1995, pp. 228-241
In recent in vitro experiments, it has been demonstrated that the 47-k
Da fragment of the talin molecule and the 32-kDa fragment of the vincu
lin molecule interact with acidic phospholipids. By using a computer a
nalysis method, we determined the hydrophobic and amphipathic stretche
s 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). Calculation
s for the 32-kDa chicken embryo vinculin fragment (residues 858-1066;
COOH-terminal region) and from nematode vinculin alignment indicate fo
r chicken embryo vinculin residues 935-978 and 1020-1040 interactions
with acidic phospholipids. Experimental confirmation has been given fo
r vinculin (residues 916-970), and future detailed experimental analys
es are now needed to support the remaining computational data.