title: [Internal symmetry of the mirror type and repeats in molecules of the membrane-bound forms of adenylate cyclase].
abstract: The analysis of mirror type internal symmetry distribution in primary structures of different types of mammalian membrane-bound adenylyl cyclases was made. The transmembrane domain clusters determining enzyme topology in membrane, a highly conservative region of cytoplasmic domains forming both catalytic and regulatory centres of adenylyl cyclases, and the functionally important regions in variable parts of their molecules (in particular, calmodulin binding regions) are shown to have symmetrical structures. These data are in conformity with a hypothesis put forward by the authors: the centres of internal symmetry may commonly either coincide with sites responsible for protein biological activity, or be spaced in the immediate vicinity of these sites. In different types of adenylyl cyclases long repeating sequences were identified. The segmentary structures were established for some enzyme subdomains. The regions containing repeats usually displayed a symmetrical structure which confirms a positive correlation between internal symmetry of amino acid sequence and its repeat distribution.
authors.affiliation: Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, St. Petersburg.
authors.forename: A O
authors.initials: AO
authors.lastname: Shpakov
authors.forename: E V
authors.initials: EV
authors.lastname: Denisov
mesh_terms: D000262:Adenylyl Cyclases / Q000737:chemistry / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D011487:Protein Conformation
chemical_list: D008565:Membrane Proteins; D000262:Adenylyl Cyclases