<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Carlson CB</submitter><funding>NCRR NIH HHS</funding><funding>NHLBI NIH HHS</funding><pagination>20069-76</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2459288</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>283(29)</volume><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 </pubmed_abstract><journal>The Journal of biological chemistry</journal><pubmed_title>Influences of the N700S thrombospondin-1 polymorphism on protein structure and stability.</pubmed_title><pmcid>PMC2459288</pmcid><funding_grant_id>HL 07899</funding_grant_id><funding_grant_id>HL 54462</funding_grant_id><funding_grant_id>S10 RR 13790</funding_grant_id><pubmed_authors>Liu Y</pubmed_authors><pubmed_authors>Keck JL</pubmed_authors><pubmed_authors>Carlson CB</pubmed_authors><pubmed_authors>Mosher DF</pubmed_authors></additional><is_claimable>false</is_claimable><name>Influences of the N700S thrombospondin-1 polymorphism on protein structure and stability.</name><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 </description><dates><release>2008-01-01T00:00:00Z</release><publication>2008 Jul</publication><modification>2026-05-01T15:41:24.91Z</modification><creation>2019-03-27T00:15:48Z</creation></dates><accession>S-EPMC2459288</accession><cross_references><pubmed>18499674</pubmed><doi>10.1074/jbc.M800223200</doi><doi>10.1074/jbc.m800223200</doi></cross_references></HashMap>