Molecular genetics of the VDAC ion channel

Structural model and sequence analysis

Michael Forte, H. Robert Guy, Carmen A. Mannella

Research output: Contribution to journalArticle

90 Citations (Scopus)

Abstract

The voltage-dependent anion-selective channel of the outer mitochondrial membrane provides a unique system in which to study the molecular basis of voltage gating of ion flow. We have cloned and sequenced a cDNA coding for this protein in yeast. From the derived amino acid sequence, we have generated a preliminary model for the secondary structure of the protein which suggests that the protein forms a "β-barrel" type structure. Comparison of the VDAC amino acid sequence with that of the bacterial porins has indicated that the two classes of molecules appear to be unrelated.

Original languageEnglish (US)
Pages (from-to)341-350
Number of pages10
JournalJournal of Bioenergetics and Biomembranes
Volume19
Issue number4
DOIs
StatePublished - Aug 1987

Fingerprint

Structural Models
Ion Channels
Sequence Analysis
Molecular Biology
Amino Acid Sequence
Voltage-Dependent Anion Channels
Secondary Protein Structure
Porins
Fungal Proteins
Mitochondrial Membranes
Complementary DNA
Ions
Proteins

Keywords

  • bacterial porins
  • gene cloning
  • secondary structure
  • sequence homology
  • Yeast VDAC

ASJC Scopus subject areas

  • Physiology
  • Cell Biology

Cite this

Molecular genetics of the VDAC ion channel : Structural model and sequence analysis. / Forte, Michael; Guy, H. Robert; Mannella, Carmen A.

In: Journal of Bioenergetics and Biomembranes, Vol. 19, No. 4, 08.1987, p. 341-350.

Research output: Contribution to journalArticle

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