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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]