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Vol 44(2010) N 6 p. 948-957;
V.P. Kutyshenko1*, L.V. Gushchina2, V.S. Khristoforov1, D.A. Prokhorov1, M.A. Timchenko1, Y.A. Kudrevatykh1, D.V. Fedyukina1, V.V. Filimonov2

NMR Structure and Dynamics of the Chimeric Protein SH3-F2

1Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region, 142290 Russia
2Institute of Protein Reseach, Russian Academy of Sciences, Pouschino, 142290 Russia

*kutyshenko@rambler.ru
Received - 2010-05-19; Accepted - 2010-06-22

In order to further elucidate structural and dynamic principles of protein self-organization and protein-ligand interactions, a new chimeric protein was designed and a genetically engineered construct was created. SH3-F2 aminoacid sequence consists of polyproline ligand mgAPPLPPYSA, GG linker, and the sequence of spectrin SH3 domain circular permutant S19-P20s. Structural and dynamic properties of the protein were studied with high-resolution NMR. According to NMR data, the tertiary structure of the chimeric protein SH3-F2 has a topology that is typical for SH3 domains in the complex with the ligand forming polyproline type II helix located in the conservative region of binding in the orientation II. The polyproline ligand closely adjoins with the protein globule and is stabilized by hydrophobic interactions. However, the interactions of the ligand and the part of globule related to SH3 domain is not too large, because the analysis of protein dynamical characteristics points to the low amplitude, high-frequency ligand tumbling relative to the slow intramolecular motions of the main globule. The constructed chimera allows carrying out further structural and thermodynamic investigations of polyproline helix properties and its interaction with regulatory domains.

SH3-domain, chimeric protein SH3-F2, 3D structure, dynamics, praline-rich peptide, protein-ligand interactions, NMR



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