4OUM

Crystal structure of human Caprin-2 C1q domain

4OUM の概要

• エントリーDOI: 10.2210/pdb4oum/pdb
• 関連するPDBエントリー: 4OUL
• 分子名称: Caprin-2, TETRAETHYLENE GLYCOL, CITRATE ANION, ... (5 entities in total)
• 機能のキーワード: c1q domain, wnt signaling, signaling protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Isoform 1: Cytoplasm. Isoform 2: Mitochondrion. Isoform 5: Mitochondrion: Q6IMN6
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16389.57

構造登録者

Song, X.,Li, L. (登録日: 2014-02-18, 公開日: 2014-10-29, 最終更新日: 2023-11-08)

主引用文献

Miao, H.,Jia, Y.,Xie, S.,Wang, X.,Zhao, J.,Chu, Y.,Zhou, Z.,Shi, Z.,Song, X.,Li, L.
Structural insights into the C1q domain of Caprin-2 in canonical Wnt signaling
J.Biol.Chem., 289:34104-34113, 2014

PubMed Abstract: Previously, we have identified Caprin-2 as a new regulator in canonical Wnt signaling through a mechanism of facilitating LRP5/6 phosphorylation; moreover, we found that its C-terminal C1q-related domain (Cap2_CRD) is required for this process. Here, we determined the crystal structures of Cap2_CRD from human and zebrafish, which both associate as a homotrimer with calcium located at the symmetric center. Surprisingly, the calcium binding-deficient mutant exists as a more stable trimer than its wild-type counterpart. Further studies showed that this Caprin-2 mutant disabled in binding calcium maintains the activity of promoting LRP5/6 phosphorylation, whereas the mutations disrupting Cap2_CRD homotrimer did impair such activity. Together, our findings suggested that the C-terminal CRD domain of Caprin-2 forms a flexible homotrimer mediated by calcium and that such trimeric assembly is required for Caprin-2 to regulate canonical Wnt signaling.

PubMed: 25331957
DOI: 10.1074/jbc.M114.591636

実験手法

X-RAY DIFFRACTION (1.491 Å)