{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Zhao YT"],"funding":["NIDCR NIH HHS","NCATS NIH HHS","NHLBI NIH HHS","NIGMS NIH HHS"],"pubmed_abstract":["Angiopoietin 1 and 2 (Ang1 and Ang2) modulate angiogenesis and vascular homeostasis through engagement of their very similar F-domain modules with the Tie2 receptor tyrosine kinase on endothelial cells. Despite this similarity in the underlying receptor binding interaction, the two angiopoietins have opposite effects: Ang1 induces phosphorylation of protein kinase B (AKT), strengthens cell-cell junctions and enhances endothelial cell survival while Ang2 antagonizes these effects <sup>1-4</sup> . To investigate the molecular basis for the opposing effects, we examined the protein kinase activation and morphological phenotypes produced by a series of computationally designed protein scaffolds presenting the Ang1 F-domain in a wide range of valencies and geometries. We find two broad phenotyp"],"journal":["bioRxiv : the preprint server for biology"],"pagination":["2020.09.19.304188"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7836102"],"repository":["biostudies-literature"],"pubmed_title":["F-domain valency determines outcome of signaling through the angiopoietin pathway."],"pmcid":["PMC7836102"],"funding_grant_id":["P01 GM081619","T90 DE021984","U01 HL099997","R01 GM097372","U01 HL099993","R01 GM083867","TL1 TR002318"],"pubmed_authors":["Ruohola-Baker H","Somasundaram L","Xavier I","Xu C","Baker D","Fallas JA","Zhao YT","Saini S","Zhou Z","Sellers DL","Mathieu J","Wrenn S","Carter L","Ueda G","Ehnes D"],"additional_accession":[]},"is_claimable":false,"name":"F-domain valency determines outcome of signaling through the angiopoietin pathway.","description":"Angiopoietin 1 and 2 (Ang1 and Ang2) modulate angiogenesis and vascular homeostasis through engagement of their very similar F-domain modules with the Tie2 receptor tyrosine kinase on endothelial cells. Despite this similarity in the underlying receptor binding interaction, the two angiopoietins have opposite effects: Ang1 induces phosphorylation of protein kinase B (AKT), strengthens cell-cell junctions and enhances endothelial cell survival while Ang2 antagonizes these effects <sup>1-4</sup> . To investigate the molecular basis for the opposing effects, we examined the protein kinase activation and morphological phenotypes produced by a series of computationally designed protein scaffolds presenting the Ang1 F-domain in a wide range of valencies and geometries. We find two broad phenotyp","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Dec","modification":"2026-04-07T22:14:54.645Z","creation":"2021-02-21T04:12:25Z"},"accession":"S-EPMC7836102","cross_references":{"pubmed":["33501432"],"doi":["10.1101/2020.09.19.304188"]}}