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Table 3 Characteristics of sequences implicated in lipid binding. The isolelectric point for the isolated peptide was calculated and the percent alpha-helix determined from the relevant crystal structure. The symbols for electrically positive residues are underlined (); those corresponding to electrically negative residues are underlined (). The characters under the amino acid sequence refer to the secondary structure; H = helix, T = hydrogen-bonded turn, S = bend, E = extended beta-strand, and B = residue in isolated beta-bridge. Residues 401–406 (KKKKSK) are not present in talin crystal structures. Helical residues are underlined ().

From: Protein-lipid interactions: correlation of a predictive algorithm for lipid-binding sites with three-dimensional structural data

Protein Residues Sequence Number Residues Isoelectric Point Helix Content Sequence Site in Protein
α-actinin 281–300 20 4.49 15/20 (75%) Helices 1–2
  720–739 20 4.66 16/20 (80%) Carboxyl-terminal portion of Helix 16
Arp2 185–202 18 10.0 13/18 (72%) Helix 1 of Actin-like Subdomain 4
CapZβ-1 134–151 18 9.62 0/18 (0%) Contains portion of β strand 6
  215–232 18 4.49 18/18 (100%) Helix 5
Talin 385–406 22 8.61 9/22 (41%) Helix 5 of Subdomain F3 of Talin-H
Vinculin 935–978 44 9.73 31/44 (70%) Domain 5, Helices 2–3 + amino-terminal portion of Helix 4
       
  1020–1040 21 4.47 20/21 (95%) Domain 5, Helix 5
  1052–1066 15    Hairpin [122]