title: [Chimeric SHA-D domain ("SH3-Bergerac"): 3D-structure and dynamics studies in solution].
abstract: Protein SHA-D of "SH3-Bergerac" chimeric proteins family was constructed by substitution of beta-turn N47-D48 in spectrin SH3-domain by KATANDKTYE amino acid sequence. Structural and dynamics properties of SHA-D in solution were studied by with the help of high-resolution NMR. The extension of SHA-D polypeptide chain in comparison with wild type of protein WT-SH3 (~ 17%) practically doesn't affect almost the total molecule topology. 3D-structure of SHA-D is practically identical to the proteins of "SH3-Bergerac" family. However there are some differences in dynamic characteristics in the region of substitution. The G52D substitution in SHA-D protein results in a destabilization of the region insertion where the conditions for conformational exchange appear. Destabilization further affects the entire SHA- D molecule making its structure more labile.
authors.forename: V S
authors.initials: VS
authors.lastname: Khristophorov
authors.forename: D A
authors.initials: DA
authors.lastname: Prokhorov
authors.forename: M A
authors.initials: MA
authors.lastname: Timchenko
authors.forename: Iu A
authors.initials: IuA
authors.lastname: Kudrevatykh
authors.forename: L V
authors.initials: LV
authors.lastname: Gushchina
authors.forename: V V
authors.initials: VV
authors.lastname: Filimonov
authors.forename: V P
authors.initials: VP
authors.lastname: Kutyshenko
mesh_terms: D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D011993:Recombinant Fusion Proteins / Q000737:chemistry* / Q000235:genetics; D018909:src Homology Domains
chemical_list: D011993:Recombinant Fusion Proteins