8IVD

COMPLEX STRUCTURE OF CD93-IGFBP7

8IVD の概要

• エントリーDOI: 10.2210/pdb8ivd/pdb
• 分子名称: Insulin-like growth factor-binding protein 7,Complement component C1q receptor (2 entities in total)
• 機能のキーワード: complex structure, immune regulation, adhesion, tumor suppression, cell adhesion
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 201317.48

構造登録者

Xu, Y.M.,Song, G.J. (登録日: 2023-03-27, 公開日: 2024-01-17, 最終更新日: 2024-10-30)

主引用文献

Xu, Y.,Sun, Y.,Zhu, Y.,Song, G.
Structural insight into CD93 recognition by IGFBP7.
Structure, 32:282-291.e4, 2024

PubMed Abstract: The CD93/IGFBP7 axis proteins are key factors expressed in endothelial cells (EC) that mediate EC angiogenesis and migration. Their upregulation contributes to tumor vascular abnormality and a blockade of this interaction promotes a favorable tumor microenvironment for therapeutic interventions. However, the interactions of these proteins with each other remain unclear. In this study, we determined a partial structure of the human CD93-IGFBP7 complex comprising the EGF domain of CD93 and the IB domain of IGFBP7. Mutagenesis studies confirmed interactions and specificities. Cellular and mouse tumor studies demonstrated the physiological relevance of the CD93-IGFBP7 interaction in EC angiogenesis. Our study provides leads for the development of therapeutic agents to precisely disrupt unwanted CD93-IGFBP7 signaling in the tumor microenvironment. Additionally, analysis of the CD93 full-length architecture provides insights into how CD93 protrudes on the cell surface and forms a flexible platform for binding to IGFBP7 and other ligands.

PubMed: 38218180
DOI: 10.1016/j.str.2023.12.011

実験手法

X-RAY DIFFRACTION (3.24 Å)