ArticleThe Journal of biological chemistry2008
Influences of the N700S thrombospondin-1 polymorphism on protein structure and stability.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 26 citations in OpenAlex.
- Variations of VEGFR2 Chemical Space: Stimulator and Inhibitory Peptides.International journal of molecular sciences · 2024Article
- Why do humans need thrombospondin-1?Journal of cell communication and signaling · 2023Review
- Pathogenesis of glaucoma: Extracellular matrix dysfunction in the trabecular meshwork-A review.Clinical & experimental ophthalmology · 2022Review
- Thrombospondin-1 Signaling Through the Calreticulin/LDL Receptor Related Protein 1 Axis: Functions and Possible Roles in Glaucoma.Frontiers in cell and developmental biology · 2022Review
- Identification of Missense Extracellular Matrix Gene Variants in a Large Glaucoma Pedigree and Investigation of the N700S Thrombospondin-1 Variant in Normal and Glaucomatous Trabecular Meshwork Cells.Current eye research · 2022Article
- Differential intolerance to loss of function and missense mutations in genes that encode human matricellular proteins.Journal of cell communication and signaling · 2021Article
- THBS1 (thrombospondin-1).Atlas of genetics and cytogenetics in oncology and haematology · 2020Article
- Thrombospondin-4 in tissue remodeling.Matrix biology : journal of the International Society for Matrix Biology · 2019Review
- An association-adjusted consensus deleterious scheme to classify homozygous Mis-sense mutations for personal genome interpretation.BioData mining · 2013Article
- Higher plasma thrombospondin-1 levels in patients with coronary artery disease and diabetes mellitus.Korean circulation journal · 2012Article
- The thrombospondins.Cold Spring Harbor perspectives in biology · 2011Review
- Interactions among stalk modules of thrombospondin-1.The Journal of biological chemistry · 2009Article
- Interactions among the epidermal growth factor-like modules of thrombospondin-1.The Journal of biological chemistry · 2009Article
- Mutations targeting intermodular interfaces or calcium binding destabilize the thrombospondin-2 signature domain.The Journal of biological chemistry · 2008Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
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 THBS-1) revealed that the impact of the Ser allele is similar in both THBS-1 and THBS-2. Structure determination of the Ser(702) THBS-2 variant in 2 mm calcium showed that repeat 1C contains two bound calcium ions as in the crystal of the Asn(702) protein, including the ion that is coordinated by Asn(702), and is associated with changes in conformation of repeat 1C and the adjacent EGF-like modules. The Ser substitution leads to the decreased ability of soluble THBS-2 signature domain protein to bind 4B6.13, a conformation-sensitive monoclonal antibody that recognizes an epitope in repeat 1C. These results indicate that although THBS harboring the Ser allele binds a full complement of calcium ions, repeat 1C is altered, leading to destabilization of surrounding structures.
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