[Chimeric SHA-D domain ("SH3-Bergerac"): 3D-structure and dynamics studies in solution].
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.
Khristophorov
V S
VS
Prokhorov
D A
DA
Timchenko
M A
MA
Kudrevatykh
Iu A
IuA
Gushchina
L V
LV
Filimonov
V V
VV
Kutyshenko
V P
VP
D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D011993:Recombinant Fusion Proteins / Q000737:chemistry* / Q000235:genetics; D018909:src Homology Domains
D011993:Recombinant Fusion Proteins