2KR3

Solution structure of SHA-D

2KR3 の概要

• エントリーDOI: 10.2210/pdb2kr3/pdb
• 関連するPDBエントリー: 2rmo
• 分子名称: Spectrin alpha chain, brain (1 entity in total)
• 機能のキーワード: alpha spectrin sh3 domain, bergerac, actin capping, actin-binding, cytoskeleton, signaling protein
• 由来する生物種: Gallus gallus (Chicken)
• 細胞内の位置: Cytoplasm, cytoskeleton: P07751
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8124.26

構造登録者

Khristoforov, V.S.,Prokhorov, D.A.,Timchenko, M.A.,Kudrevatykh, Y.A.,Gushchina, L.V.,Filimonov, V.V.,Kutyshenko, V.P. (登録日: 2009-12-03, 公開日: 2010-09-15, 最終更新日: 2024-05-01)

主引用文献

Khristoforov, V.S.,Prokhorov, D.A.,Timchenko, M.A.,Kudrevatykh, Y.A.,Gushchina, L.V.,Filimonov, V.V.,Kutyshenko, V.P.
Chimeric SHA-D domain "SH3-Bergerac": 3D structure and dynamics studies
Russ.J.Bioorganic Chem., 36:468-476, 2010

PubMed Abstract: 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.

PubMed: 20823919
DOI: 10.1134/S1068162010040059

実験手法

SOLUTION NMR