{"database":"biostudies-literature","file_versions":[],"scores":{"citationCount":0,"reanalysisCount":0,"viewCount":59,"searchCount":0},"additional":{"omics_type":["Unknown"],"volume":["109(8)"],"submitter":["Yeo GC"],"pubmed_abstract":["The tropoelastin monomer undergoes stages of association by coacervation, deposition onto microfibrils, and cross-linking to form elastic fibers. Tropoelastin consists of an elastic N-terminal coil region and a cell-interactive C-terminal foot region linked together by a highly exposed bridge region. The bridge region is conveniently positioned to modulate elastic fiber assembly through association by coacervation and its proximity to dominant cross-linking domains. Tropoelastin constructs that either modify or remove the entire bridge and downstream regions were assessed for elastogenesis. These constructs focused on a single alanine substitution (R515A) and a truncation (M155n) at the highly conserved arginine 515 site that borders the bridge. Each form displayed less efficient coacervation, impaired hydrogel formation, and decreased dermal fibroblast attachment compared to wild-type tropoelastin. The R515A mutant protein additionally showed reduced elastic fiber formation upon addition to human retinal pigmented epithelium cells and dermal fibroblasts. The small-angle X-ray scattering nanostructure of the R515A mutant protein revealed greater conformational flexibility around the bridge and C-terminal regions. This increased flexibility of the R515A mutant suggests that the tropoelastin R515 residue stabilizes the structure of the bridge region, which is critical for elastic fiber assembly."],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pagination":["2878-83"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3286909"],"repository":["biostudies-literature"],"pubmed_title":["Tropoelastin bridge region positions the cell-interactive C terminus and contributes to elastic fiber assembly."],"pmcid":["PMC3286909"],"pubmed_authors":["Baldock C","Tuukkanen A","Weiss AS","Dyksterhuis LB","Yeo GC","Matthews J","Roessle M","Wise SG","Mithieux SM"],"view_count":["59"],"additional_accession":[]},"is_claimable":false,"name":"Tropoelastin bridge region positions the cell-interactive C terminus and contributes to elastic fiber assembly.","description":"The tropoelastin monomer undergoes stages of association by coacervation, deposition onto microfibrils, and cross-linking to form elastic fibers. Tropoelastin consists of an elastic N-terminal coil region and a cell-interactive C-terminal foot region linked together by a highly exposed bridge region. The bridge region is conveniently positioned to modulate elastic fiber assembly through association by coacervation and its proximity to dominant cross-linking domains. Tropoelastin constructs that either modify or remove the entire bridge and downstream regions were assessed for elastogenesis. These constructs focused on a single alanine substitution (R515A) and a truncation (M155n) at the highly conserved arginine 515 site that borders the bridge. Each form displayed less efficient coacervation, impaired hydrogel formation, and decreased dermal fibroblast attachment compared to wild-type tropoelastin. The R515A mutant protein additionally showed reduced elastic fiber formation upon addition to human retinal pigmented epithelium cells and dermal fibroblasts. The small-angle X-ray scattering nanostructure of the R515A mutant protein revealed greater conformational flexibility around the bridge and C-terminal regions. This increased flexibility of the R515A mutant suggests that the tropoelastin R515 residue stabilizes the structure of the bridge region, which is critical for elastic fiber assembly.","dates":{"release":"2012-01-01T00:00:00Z","publication":"2012 Feb","modification":"2020-11-19T12:22:09Z","creation":"2019-03-27T00:49:27Z"},"accession":"S-EPMC3286909","cross_references":{"pubmed":["22328151"],"doi":["10.1073/pnas.1111615108"]}}