2KXD

The structure of SH3-F2

2KXD の概要

• エントリーDOI: 10.2210/pdb2kxd/pdb
• 関連するPDBエントリー: 1TUC 2JMC
• NMR情報: BMRB: 17089
• 分子名称: 11-mer peptide,Spectrin alpha chain, non-erythrocytic 1,Spectrin alpha chain, non-erythrocytic 1 (1 entity in total)
• 機能のキーワード: alpha spectrin sh3 domain, spc-s19p20s circular permutant, signaling protein
• 由来する生物種: synthetic construct; 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8097.24

構造登録者

Kutyshenko, V.P.,Gushchina, L.V.,Khristoforov, V.S.,Prokhorov, D.A.,Timchenko, M.A.,Kudrevatykh, I.u.A.,Fedyukina, D.V.,Filimonov, V.V. (登録日: 2010-04-30, 公開日: 2011-04-20, 最終更新日: 2024-05-01)

主引用文献

Kutyshenko, V.P.,Gushchina, L.V.,Khristoforov, V.S.,Prokhorov, D.A.,Timchenko, M.A.,Kudrevatykh, I.u.A.,Fediukina, D.V.,Filimonov, V.V.
NMR structure and dynamics of the chimeric protein SH3-F2
Mol.Biol.(Engl.Transl.), 44:948-957, 2010

PubMed Abstract: 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.

PubMed: 21290828
DOI: 10.1134/S0026893310060129

実験手法

SOLUTION NMR