title: Intermolecular homologies of human interferon-alpha.
abstract: Human interferon-alpha 2 (IFN) was analyzed by homology search computer program with the use of protein primary structures data bases. Results indicate that four domains with heightened ability to form homology pairs with different proteins exist in the IFN molecule. These domains occupy regions 35-56, 72-85, 97-110 and 124-136, mainly between the alpha-helical cylinders on the tertiary structure models. Additionally, results show in IFN structure the presence of amino-acid motifs that create the opportunity for this cytokine to influence directly the processes of DNA functioning in cell nuclei.
authors.affiliation: Center of Medical Biotechnology, Moscow, Russia.
authors.forename: F E
authors.initials: FE
authors.lastname: Romantsev
authors.forename: N N
authors.initials: NN
authors.lastname: Khodarev
authors.forename: I I
authors.initials: II
authors.lastname: Votrin
mesh_terms: D000595:Amino Acid Sequence; D006801:Humans; D016898:Interferon-alpha / Q000737:chemistry / Q000235:genetics*; D016350:Leucine Zippers / Q000235:genetics; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011518:Proto-Oncogene Proteins / Q000235:genetics; D012689:Sequence Homology, Nucleic Acid; D012984:Software
chemical_list: D016898:Interferon-alpha; D011518:Proto-Oncogene Proteins