{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Xu Y"],"funding":["Science and Technology Commission of Shanghai Municipality","National Natural Science Foundation of China","NCI NIH HHS","National Institutes of Health"],"pagination":["282-291.e4"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12364601"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["32(3)"],"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<sub>1</sub> 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 dis"],"journal":["Structure (London, England : 1993)"],"pubmed_title":["Structural insight into CD93 recognition by IGFBP7."],"pmcid":["PMC12364601"],"funding_grant_id":["R01 CA269644","R01 CA279398","32171215","R01CA279398","R01CA269644","R01CA258302","R01 CA258302","21JC1402400"],"pubmed_authors":["Zhu Y","Sun Y","Song G","Xu Y"],"additional_accession":[]},"is_claimable":false,"name":"Structural insight into CD93 recognition by IGFBP7.","description":"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<sub>1</sub> 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 dis","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Mar","modification":"2026-05-29T14:23:41.474Z","creation":"2026-04-08T05:03:23.057Z"},"accession":"S-EPMC12364601","cross_references":{"pubmed":["38218180"],"doi":["10.1016/j.str.2023.12.011"]}}