Helix-helix interfaces and ligand binding.

J Theor Biol

The School of Theoretical Modeling, Department of Biophysics, PO Box 15676, Chevy Chase, MD 20825, USA.

Published: August 2011

AI Article Synopsis

  • - Helix-helix parallel interfaces rely on specific amino acid combinations, particularly at core positions (a and d), which affect the angles between helices in proteins.
  • - The framework was successfully used to predict interhelical angles in 62 different proteins, with accurate results for 58 of them.
  • - The study found a correlation between interhelical angles and the conformation of various ligands related to glutathione S-transferase.

Article Abstract

Helix-helix parallel interfaces can be characterized by certain combinations of amino acids, which repeatedly occur at core positions a and d (leucine zipper nomenclature) in homologous and nonhomologous proteins and influence interhelical angles. Applied for the prediction of interhelical angles in glutathione S-transferase, intracellular chloride channel and annexin molecules from various sources, correct results were achieved in 58 out of 62 proteins. Interhelical angles are found to correlate with the conformation of the glutathione S-transferase ligands glutathione, s-hexylglutathione, glutathione sulfonic acid, and glutathione-s-dinitrobenzene.

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http://dx.doi.org/10.1016/j.jtbi.2011.05.014DOI Listing

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