title: [Spatial organization of the globular fragment of calmodulin. 2. Conformational analysis of packing of two domains].
abstract: Theoretical conformational analysis of possible packing of two alpha-helical strands has been performed for the amino-acid sequence of N-terminal domains of CaM. It has been shown, that side chains of the antiparallel alpha-strands can interpenetrate and form a structure of the "knobs into holes" type. Such packing is profitable in the energy terms and can serve as an element of supersecondary structure, named "alpha-barrel". A possible conformational mechanism of CaM activation by Ca2+ is discussed in terms of the proposed model.
authors.forename: A Iu
authors.initials: AIu
authors.lastname: Avanov
mesh_terms: D000595:Amino Acid Sequence; D002118:Calcium / Q000737:chemistry; D002147:Calmodulin / Q000737:chemistry*; D008956:Models, Chemical; D008969:Molecular Sequence Data; D011487:Protein Conformation
chemical_list: D002147:Calmodulin; D002118:Calcium
vernacular_title: Issledovanie prostranstvennoĭ organizatsii globuliarnogo fragmenta kalmodulina. 2. Konformatsionnyĭ analiz ukladki dvukh domenov.