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

Natalia Bogatcheva, Nikolai B. Gusev

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

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
Volume363
Issue number3
DOIs
StatePublished - Apr 24 1995
Externally publishedYes

Fingerprint

Calmodulin-Binding Proteins
Phospholipids
Binding Sites
Microfilament Proteins
Smooth Muscle
Muscle
Membranes
Lipids
calponin
Proteins

Keywords

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

ASJC Scopus subject areas

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

Cite this

Computer-assistant prediction of phospholipid binding sites of caldesmon and calponin. / Bogatcheva, Natalia; Gusev, Nikolai B.

In: FEBS Letters, Vol. 363, No. 3, 24.04.1995, p. 269-272.

Research output: Contribution to journalArticle

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N2 - 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.

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