Computer‐assistant prediction of phospholipid binding sites of caldesmon and calponin

FEBS Letters

Gusev, Nikolai B.¹  Bogatcheva, Natalia V.¹ 

[1] Department of Biochemistry, School of Biology, Moscow State University, Moscow 119899, Russian Federation

关键词: Caldesmon;    Calponin;    Phospholipid;    Sequence analysis;    Structure prediction;    Calmodulin;   

DOI  :  10.1016/0014-5793(95)00328-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The primary structure of smooth muscle caldesmon and calponin was screened for the presence of amphiphilic α-helices which can participate in the formation of protein-lipid contacts. Only one caldesmon segment (residues 645–660) having a predominantly α-helical structure and high hydrophobic moment satisfies all criteria for a surface-seeking helix and is predicted to be involved in the caldesmon-phospholipid interaction. This prediction agrees with experimental results indicating that one of the caldesmon-phospholipid binding sites is located in the sequence 628–658 [Bogatcheva et al. (1994) FEBS Lett. 342, 176]. Two segments of calponin (residues 45–55 and 85–95) exhibit high hydrophobic moments and the sequence 85–95 is characterized by a high probability of α-helix formation. This may suggest that at least one of these segments could facilitate the calponin-phospholipid interaction and that calponin, as with many other actin binding proteins, is able to interact with membranes.

【 授权许可】

Unknown