title: Helix-helix interfaces and ligand binding.
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.
authors.affiliation: The School of Theoretical Modeling, Department of Biophysics, PO Box 15676, Chevy Chase, MD 20825, USA. info@schtm.org
authors.forename: Natalya
authors.initials: N
authors.lastname: Kurochkina
authors.forename: Tsering
authors.initials: T
authors.lastname: Choekyi
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D017302:Annexins / Q000235:genetics; D018118:Chloride Channels / Q000235:genetics; D005982:Glutathione Transferase / Q000235:genetics; D006801:Humans; D016350:Leucine Zippers; D008024:Ligands; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation
chemical_list: D017302:Annexins; D018118:Chloride Channels; D008024:Ligands; D005982:Glutathione Transferase