2ROT

Structure of chimeric variant of SH3 domain- SHH

2ROT の概要

• エントリーDOI: 10.2210/pdb2rot/pdb
• NMR情報: BMRB: 11043
• 分子名称: Spectrin alpha chain, brain (1 entity in total)
• 機能のキーワード: sh3, chimeric protein, alpha-spectrin, actin capping, actin-binding, calcium, calmodulin-binding, cytoplasm, cytoskeleton, phosphoprotein, sh3 domain, protein binding
• 由来する生物種: Gallus gallus (Chicken)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8136.35

構造登録者

Kutyshenko, N.P.,Prokhorov, D.A.,Timchenko, M.A.,Kudrevatykh, Y.A.,Gushchina, L.V.,Khristoforov, V.S.,Filimonov, V.V. (登録日: 2008-04-10, 公開日: 2009-04-28, 最終更新日: 2024-05-15)

主引用文献

Kutyshenko, V.P.,Prokhorov, D.A.,Timchenko, M.A.,Kudrevatykh, Y.A.,Gushchina, L.V.,Khristoforov, V.S.,Filimonov, V.V.,Uversky, V.N.
Solution structure and dynamics of the chimeric SH3 domains, SHH- and SHA-"Bergeracs".
Biochim.Biophys.Acta, 1794:1813-1822, 2009

PubMed Abstract: Two chimeric proteins, SHcapital EN, Cyrillic and SHA of the "SH3-Bergerac" family (where the beta-turn N47D48 in spectrin SH3 domain was substituted for KITVNGKTYE or KATANGKTYE sequences, respectively), were analyzed by high-resolution NMR to resolve their spatial structures and to analyze their dynamics. Although the presence of a stable beta-hairpin in the region of the insertion was confirmed, the introduced extension of the polypeptide chain in SHcapital EN, Cyrillic (approximately 17%) practically did not affect the total molecule topology. Interestingly, the introduced beta-hairpin had higher mobility in comparison with other protein regions. Finally, we performed a disorder prediction with the PONDR VSL2 algorithm and discovered that the inserted beta-hairpin in both SHH and SHA proteins exhibited significant propensity for intrinsic disorder and therefore for high mobility. In agreement with the experimental data, the predisposition for the increased intramolecular mobility was noticeably higher in SHA.

PubMed: 19732853
DOI: 10.1016/j.bbapap.2009.08.021

実験手法

SOLUTION NMR