5ZRZ

Crystal Structure of EphA5/SAMD5 Complex

5ZRZ の概要

• エントリーDOI: 10.2210/pdb5zrz/pdb
• 分子名称: Ephrin type-A receptor 5, Sterile alpha motif domain-containing protein 5 (3 entities in total)
• 機能のキーワード: sam domain, heterodimer, signaling protein, cell signaling, receptor, transmembrane, tyrosine-protein kinase, cell adhesion, protein binding
• 由来する生物種: Mus musculus (Mouse); 詳細
• 細胞内の位置: Cell membrane ; Single-pass type I membrane protein : Q60629
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 16694.10

構造登録者

Wang, Y.,Shang, Y.,Li, J.,Chen, W.,Li, G.,Wan, J.,Liu, W.,Zhang, M. (登録日: 2018-04-25, 公開日: 2018-05-30, 最終更新日: 2023-11-22)

主引用文献

Wang, Y.,Shang, Y.,Li, J.,Chen, W.,Li, G.,Wan, J.,Liu, W.,Zhang, M.
Specific Eph receptor-cytoplasmic effector signaling mediated by SAM-SAM domain interactions.
Elife, 7:-, 2018

PubMed Abstract: The Eph receptor tyrosine kinase (RTK) family is the largest subfamily of RTKs playing critical roles in many developmental processes such as tissue patterning, neurogenesis and neuronal circuit formation, angiogenesis, etc. How the 14 Eph proteins, via their highly similar cytoplasmic domains, can transmit diverse and sometimes opposite cellular signals upon engaging ephrins is a major unresolved question. Here, we systematically investigated the bindings of each SAM domain of Eph receptors to the SAM domains from SHIP2 and Odin, and uncover a highly specific SAM-SAM interaction-mediated cytoplasmic Eph-effector binding pattern. Comparative X-ray crystallographic studies of several SAM-SAM heterodimer complexes, together with biochemical and cell biology experiments, not only revealed the exquisite specificity code governing Eph/effector interactions but also allowed us to identify SAMD5 as a new Eph binding partner. Finally, these Eph/effector SAM heterodimer structures can explain many Eph SAM mutations identified in patients suffering from cancers and other diseases.

PubMed: 29749928
DOI: 10.7554/eLife.35677

実験手法

X-RAY DIFFRACTION (1.89 Å)