2RMO

Solution structure of alpha-spectrin_SH3-bergerac from Chicken

2RMO の概要

• エントリーDOI: 10.2210/pdb2rmo/pdb
• NMR情報: BMRB: 11026
• 分子名称: Spectrin alpha chain, brain (1 entity in total)
• 機能のキーワード: sh3, bergerac, actin capping, actin-binding, calcium, calmodulin-binding, cytoplasm, cytoskeleton, membrane, phosphorylation, sh3 domain, 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: 8066.22

構造登録者

Kutyshenko, V.P.,Prokhorov, D.A.,Timchenko, M.A.,Kudrevatykh, Y.A.,Fedyukina, D.V.,Gushchina, L.V.,Khristoforov, V.S.,Filimonov, V.V. (登録日: 2007-11-07, 公開日: 2008-09-30, 最終更新日: 2024-05-29)

主引用文献

Prokhorov, D.A.,Timchenko, M.A.,Kudrevatykh, Y.A.,Fedyukina, D.V.,Gushchina, L.V.,Khristoforov, V.S.,Filimonov, V.V.,Kutyshenko, V.P.
Study of the structure and dynamics of a chimeric variant of the SH3 domain (SHA-Bergerac) by NMR spectroscopy
Russ.J.Bioorganic Chem., 34:578-585, 2008

PubMed Abstract: A structural-dynamic study of one of the chimeric proteins (SHA) belonging to the SH3-Bergerac family and containing the KATANGKTYE sequence instead of the N47D48 beta-turn in the spectrin SH3 domain was carried out by high resolution NMR spectroscopy. The spatial structure of the protein was determined and its dynamics in solution was investigated on the basis of the NMR data. The elongation of the SHA polypeptide chain in comparison with the WT-SH3 original protein (by ~17%) exerts practically no effect on the general topology of the molecule. The presence of a stable beta-hairpin in the region of insertion was confirmed. This hairpin was shown to have a higher mobility in comparison with other regions of the protein.

PubMed: 19060939
DOI: 10.1134/S1068162008050075

実験手法

SOLUTION NMR