2YOQ

Structure of FAM3B PANDER E30 construct

2YOQ の概要

• エントリーDOI: 10.2210/pdb2yoq/pdb
• 関連するPDBエントリー: 2YOP
• 分子名称: PROTEIN FAM3B, GLYCEROL (3 entities in total)
• 機能のキーワード: apoptosis, diabetes, ilei, emt
• 由来する生物種: MUS MUSCULUS (MOUSE)
• 細胞内の位置: Secreted (By similarity): Q9D309
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 72198.99

構造登録者

Johansson, P.,Bernstrom, J.,Gorman, T.,Oster, L.,Backstrom, S.,Schweikart, F.,Xu, B.,Xue, Y.,Holmberg Schiavone, L. (登録日: 2012-10-26, 公開日: 2013-01-30, 最終更新日: 2024-11-06)

主引用文献

Johansson, P.,Bernstrom, J.,Gorman, T.,Oster, L.,Backstrom, S.,Schweikart, F.,Xu, B.,Xue, Y.,Schiavone, L.H.
Fam3B Pander and Fam3C Ilei Represent a Distinct Class of Signaling Molecules with a Non-Cytokine-Like Fold.
Structure, 21:306-, 2013

PubMed Abstract: The FAM3 superfamily is predicted to contain classical four-helix bundle cytokines, featuring a typical up-up-down-down fold. Two members of FAM3 have been extensively studied. FAM3B PANDER has been shown to regulate glucose homeostasis and β cell function, whereas the homologous FAM3C ILEI has been shown to be involved in epithelial-mesenchymal transition and cancer. Here, we present a three-dimensional structure of a FAM3 protein, murine PANDER. Contrary to previous suggestions, PANDER exhibits a globular β-β-α fold. The structure is composed of two antiparallel β sheets lined by three short helices packing to form a highly conserved water-filled cavity. The fold shares no relation to the predicted four-helix cytokines but is conserved throughout the FAM3 superfamily. The available biological data and the unexpected new fold indicate that FAM3 PANDER and ILEI could represent a new structural class of signaling molecules, with a different mode of action compared to the traditional four-helix bundle cytokines.

PubMed: 23333428
DOI: 10.1016/J.STR.2012.12.009

実験手法

X-RAY DIFFRACTION (2.35 Å)