6CPJ

Solution structure of SH3 domain from Shank2

6CPJ の概要

• エントリーDOI: 10.2210/pdb6cpj/pdb
• NMR情報: BMRB: 30437
• 分子名称: SH3 and multiple ankyrin repeat domains protein 2 (1 entity in total)
• 機能のキーワード: psd, scaffold protein, postsynaptic density, protein binding
• 由来する生物種: Rattus norvegicus (Rat)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6741.67

構造登録者

Ishida, H.,Vogel, H.J. (登録日: 2018-03-13, 公開日: 2018-08-15, 最終更新日: 2024-05-01)

主引用文献

Ishida, H.,Skorobogatov, A.,Yamniuk, A.P.,Vogel, H.J.
Solution structures of the SH3 domains from Shank scaffold proteins and their interactions with Cav1.3 calcium channels.
FEBS Lett., 592:2786-2797, 2018

PubMed Abstract: Shank proteins are abundant scaffold proteins in the postsynaptic density (PSD) region of brain synapses. Mutations in Shank proteins are associated with autism, schizophrenia, and Alzheimer's disease. To gain insights into Shank protein interactions at the PSD, we determined the solution structures of the src homology 3 (SH3) domains of all three mammalian Shank proteins. Our findings indicate that they have identical and typical SH3 folding motifs, but unusual target-binding pockets. An investigation into the interaction between the Shank SH3 domains and the proline-rich region of the Cav1.3 calcium channel revealed an atypical interaction in which the highly acidic specificity binding pocket of the SH3 domains binds to a Cav1.3 region containing a cluster of three Arg residues. Our study provides insights into Shank SH3-mediated interactions.

PubMed: 30058071
DOI: 10.1002/1873-3468.13209

実験手法

SOLUTION NMR