8IVD
COMPLEX STRUCTURE OF CD93-IGFBP7
Summary for 8IVD
| Entry DOI | 10.2210/pdb8ivd/pdb |
| Descriptor | Insulin-like growth factor-binding protein 7,Complement component C1q receptor (2 entities in total) |
| Functional Keywords | complex structure, immune regulation, adhesion, tumor suppression, cell adhesion |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 201317.48 |
| Authors | Xu, Y.M.,Song, G.J. (deposition date: 2023-03-27, release date: 2024-01-17, Last modification date: 2024-10-30) |
| Primary citation | Xu, Y.,Sun, Y.,Zhu, Y.,Song, G. Structural insight into CD93 recognition by IGFBP7. Structure, 32:282-291.e4, 2024 Cited by 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: 38218180DOI: 10.1016/j.str.2023.12.011 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.24 Å) |
Structure validation
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