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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.
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D A Prokhorov, and
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V P Kutyshenko
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Biophysical chemistry,
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V P Kutyshenko
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V S Khristophorov, and
D A Prokhorov, and
M A Timchenko, and
Iu A Kudrevatykh, and
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V P Kutyshenko
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V P Kutyshenko
May 2013,
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D A Prokhorov, and
M A Timchenko, and
Iu A Kudrevatykh, and
L V Gushchina, and
V V Filimonov, and
V P Kutyshenko
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Journal of structural biology,
V S Khristophorov, and
D A Prokhorov, and
M A Timchenko, and
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L V Gushchina, and
V V Filimonov, and
V P Kutyshenko
June 2001,
Nature structural biology,
V S Khristophorov, and
D A Prokhorov, and
M A Timchenko, and
Iu A Kudrevatykh, and
L V Gushchina, and
V V Filimonov, and
V P Kutyshenko
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