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Publication Abstract from PubMed

For the further elucidation of structural and dynamic principles of protein self-organization and protein-ligand interactions the design of new chimeric protein SH3-F2 was made and genetically engineered construct was created. The 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 dynamics properties of the protein were studied by high-resolution NMR. According to NMR data the tertiary structure of the chimeric protein SH3-F2 has the topology which is typical of 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 interaction of ligand and the part of globule relative to SH3 domain is not too large because the analysis of protein dynamic characteristics points to the low amplitude, high-frequency ligand tumbling in relation to the slow intramolecular motions of the main globule. The constructed chimera permits to carry out further structural and thermodynamic investigations of polyproline helix properties and its interaction with regulatory domains.

[NMR structure and dynamics of the chimeric protein SH3-F2].,Kutyshenko VP, Gushchina LV, Khristoforov VS, Prokhorov DA, Timchenko MA, Kudrevatykh IuA, Fediukina DV, Filimonov VV Mol Biol (Mosk). 2010 Nov-Dec;44(6):1064-74. PMID:21290828^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.