3SEI

Crystal Structure of Caskin1 Tandem SAMs

3SEI の概要

• エントリーDOI: 10.2210/pdb3sei/pdb
• 関連するPDBエントリー: 3SEN
• 分子名称: Caskin-1, SULFATE ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: sam domain, protein-protein interaction, signaling protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm (By similarity): Q8WXD9
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34138.62

構造登録者

Stafford, R.L.,Bowie, J.U. (登録日: 2011-06-10, 公開日: 2011-12-14, 最終更新日: 2023-09-13)

主引用文献

Stafford, R.L.,Hinde, E.,Knight, M.J.,Pennella, M.A.,Ear, J.,Digman, M.A.,Gratton, E.,Bowie, J.U.
Tandem SAM domain structure of human Caskin1: a presynaptic, self-assembling scaffold for CASK.
Structure, 19:1826-1836, 2011

PubMed Abstract: The synaptic scaffolding proteins CASK and Caskin1 are part of the fibrous mesh of proteins that organize the active zones of neural synapses. CASK binds to a region of Caskin1 called the CASK interaction domain (CID). Adjacent to the CID, Caskin1 contains two tandem sterile α motif (SAM) domains. Many SAM domains form polymers so they are good candidates for forming the fibrous structures seen in the active zone. We show here that the SAM domains of Caskin1 form a new type of SAM helical polymer. The Caskin1 polymer interface exhibits a remarkable segregation of charged residues, resulting in a high sensitivity to ionic strength in vitro. The Caskin1 polymers can be decorated with CASK proteins, illustrating how these proteins may work together to organize the cytomatrix in active zones.

PubMed: 22153505
DOI: 10.1016/j.str.2011.09.018

実験手法

X-RAY DIFFRACTION (2.4 Å)