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