Thrombospondin 3 Is a Pentameric Molecule Held Together by Interchain Disulfide Linkage Involving Two Cysteine Residues
| Autor: | Aziz Qabar, Laura H. Derick, Jack Lawler, Vishva Dixit |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Protein Conformation
Disulfide Linkage Stereochemistry DNA Mutational Analysis Trimer Biochemistry Oligomer Mice chemistry.chemical_compound Animals Matrilin Proteins Cysteine Disulfides Thrombospondins Molecular Biology Glycoproteins Sequence Deletion Cartilage oligomeric matrix protein Extracellular Matrix Proteins Thrombospondin biology Mutagenesis Cell Biology Recombinant Proteins Models Chemical chemistry biology.protein Oxidation-Reduction |
| Zdroj: | Journal of Biological Chemistry. 270:12725-12729 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.270.21.12725 |
| Popis: | The thrombospondins (TSPs) are a family of 5 distinct gene products designated TSP1, -2, -3, -4, and COMP, for cartilage oligomeric matrix protein. TSP1, the prototypical member, is a trimeric extracellular matrix molecule implicated in cell migration and development. TSP1 trimer formation is mediated by interchain disulfide linkage involving two NH2-terminal cysteines. TSP3, a recent addition to the family, is a developmentally regulated heparin binding protein that is similar in sequence to the COOH terminus of TSP1 but has a distinct NH2 terminus. This has raised the question of the oligomeric nature of TSP3 and identification of the cysteine residues involved in oligomer formation. We demonstrate, using a combination of deletional and site-directed mutagenesis and rotary shadowing electron microscopy, that TSP3, like TSP4 and COMP, is a pentameric molecule. TSP3 is held together by interchain disulfide linkage involving just two cysteine residues, Cys-245 and Cys-248. |
| Databáze: | OpenAIRE |
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