NMR structure and dynamics of the chimeric protein SH3-F2 |
| |
Authors: | V P Kutyshenko L V Gushchina V S Khristoforov D A Prokhorov M A Timchenko Yu A Kudrevatykh D V Fedyukina V V Filimonov |
| |
Institution: | 1.Institute of Theoretical and Experimental Biophysics,Russian Academy of Science,Pushchino, Moscow region,Russia;2.Institute of Protein Research,Russian Academy of Science,Pushchino, Moscow region,Russia |
| |
Abstract: | 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 amino acid 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. |
| |
Keywords: | |
本文献已被 SpringerLink 等数据库收录! |
|