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

Natalia V. Bogatcheva, Nikolai B. Gusev

Research output: Contribution to journalArticle

12 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)269-272
Number of pages4
JournalFEBS Letters
Issue number3
StatePublished - Apr 24 1995
Externally publishedYes


  • Caldesmon
  • Calmodulin
  • Calponin
  • Phospholipid
  • Sequence analysis
  • Structure prediction

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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