{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Carlson CB"],"funding":["NCRR NIH HHS","NHLBI NIH HHS"],"pagination":["20069-76"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2459288"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["283(29)"],"pubmed_abstract":["Thrombospondins (THBSs) are multimodular, secreted proteins characterized by a signature domain comprising a unique set of 13 calcium-binding repeats flanked by epidermal growth factor (EGF)-like and lectin-like modules. A polymorphism that changes a conserved Asn to Ser at residue 700 in the most N-terminal calcium-binding repeat of THBS-1 (repeat 1C) is found in 8-10% of European populations and has been linked to increased risk of premature coronary artery disease. The Ser substitution leads to altered stability in the EGF-like and wire modules of the THBS-1 signature domain as assessed by differential scanning calorimetry carried out in 2 mm or 200 mum calcium. Studies of the melting profiles of the THBS-2 signature domain proteins with Asn or Ser at position 702 (homologous to 700 in "],"journal":["The Journal of biological chemistry"],"pubmed_title":["Influences of the N700S thrombospondin-1 polymorphism on protein structure and stability."],"pmcid":["PMC2459288"],"funding_grant_id":["HL 07899","HL 54462","S10 RR 13790"],"pubmed_authors":["Liu Y","Keck JL","Carlson CB","Mosher DF"],"additional_accession":[]},"is_claimable":false,"name":"Influences of the N700S thrombospondin-1 polymorphism on protein structure and stability.","description":"Thrombospondins (THBSs) are multimodular, secreted proteins characterized by a signature domain comprising a unique set of 13 calcium-binding repeats flanked by epidermal growth factor (EGF)-like and lectin-like modules. A polymorphism that changes a conserved Asn to Ser at residue 700 in the most N-terminal calcium-binding repeat of THBS-1 (repeat 1C) is found in 8-10% of European populations and has been linked to increased risk of premature coronary artery disease. The Ser substitution leads to altered stability in the EGF-like and wire modules of the THBS-1 signature domain as assessed by differential scanning calorimetry carried out in 2 mm or 200 mum calcium. Studies of the melting profiles of the THBS-2 signature domain proteins with Asn or Ser at position 702 (homologous to 700 in ","dates":{"release":"2008-01-01T00:00:00Z","publication":"2008 Jul","modification":"2026-05-01T15:41:24.91Z","creation":"2019-03-27T00:15:48Z"},"accession":"S-EPMC2459288","cross_references":{"pubmed":["18499674"],"doi":["10.1074/jbc.M800223200","10.1074/jbc.m800223200"]}}