Table 2 Computationally determined sites of probable lipid binding. A matrix algorithm [11] was used to identify probable lipid-binding sites in the following cytoskeletal proteins; α-actinin [14], Arp2 [16], CapZβ-1 (submitted, TBMM), Talin [12-13, 121] and Vinculin [14]. In-vitro experimental support for the computationally predicted sites for α-Actinin, Arp2, Talin, and Vinculin (site 935–978) was obtained from a variety of techniques including hydrophobic labeling, differential scanning calorimetry (DSC), Langmuir Blodgett (film balance), T-jump, CD spectroscopy, cryo-electron microscopy (EM), FTIR, and isothermal titration calorimetry.
Protein | Sequence Residues | Species | Sequence | Experimental (in-vitro) Validation |
|---|---|---|---|---|
α-actinin | 281–300 | Gallus gallus | EKLASDLLEWIRRTIPWLEN Residues (287–306) of 1HCI | DSC, Centrifugation, SDS-PAGE [14] |
|  | 720–739 | Gallus gallus | QLLTTIARTINEVENQILTR Residues (726–745) of 1HCI | DSC, Centrifugation, SDS-PAGE [14] |
Arp2 | 185–202 | A. castellanii | RDVTRYLIKLLLLRGYVF | DSC, Film Balance, Temperature Jump [16] |
CapZβ-1 | 134–151 | Homo sapiens | IKKAGDGSKKIKGCWDSI | No data |
|  | 215–232 | Homo sapiens | RLVEDMENKIRSTLNEIY | No data |
Talin | 385–406 | M. musculatus | GEQIAQLIAGYIDIILKKKKSK | Isothermal Titration Calorimetry, Monolayer Expansion, CD-spectroscopy [15]; FTIR [86] Resonance energy transfer, Cryo-EM [90] |
Vinculin | 935–978 | Gallus gallus | RLVRGGSGNKRALIQCAKDIAKASDEVT RLAKEVAKQCTDKRIR | Co-sedimentation, Hydrophobic Photolabeling [102] |
|  | 1020–1040 | Gallus gallus | TEMLVHNAQNLMQSVKETVRE | No data |
|  | 1052–1066 | Homo sapiens | AGFTLRWVRKTPWYQ | No data |