title: [Structural-functional analysis of the complex between phosphorylase B and adenosine-5'-chloromethylphosphonate].
abstract: A complex of phosphorylase B with a tritium-containing AMP analogue, adenosine-5'-chloromethylphosphonate, was obtained. It is found on the basis of the results of the determination of N- and C-terminal amino acids, amino acid composition and sequence, that the peptide 1, modified by adenosine-5'-chloromethylphosphonate, corresponds to the fragment 185-191 in the primary structure of phosphorylase B, and is probably located in the allosteric center of the enzyme. The peptide 2, which is bound with the AMP analogue and corresponds to the fragment 795-798, is suggested to be located at the site of binding the second AMP molecule. The arginine residue 184 is discussed as a possible functional amino acid protein interacting with 5'-phosphate AMP group.
mesh_terms: D000249:Adenosine Monophosphate / Q000031:analogs & derivatives* / Q000378:metabolism; D000495:Allosteric Site; D000595:Amino Acid Sequence; D001120:Arginine; D001665:Binding Sites; D010763:Phosphorylase b / Q000378:metabolism*; D006005:Phosphorylases / Q000378:metabolism*; D013329:Structure-Activity Relationship
chemical_list: D000249:Adenosine Monophosphate; D001120:Arginine; D010763:Phosphorylase b; D006005:Phosphorylases
vernacular_title: Strukturno-funktsional'nyĭ analiz kompleksa fosforilazy B s adenozin-5'-khlormentilfosfonatom.