Basement Membrane Protein BM-40
Erhard Hohenester
Imperial College, Department of Biological Sciences, London, UK
Search for more papers by this authorRupert Timpl
Max-Planck-Institut für Biochemie, Martinsried, Germany
Search for more papers by this authorErhard Hohenester
Imperial College, Department of Biological Sciences, London, UK
Search for more papers by this authorRupert Timpl
Max-Planck-Institut für Biochemie, Martinsried, Germany
Search for more papers by this authorAbstract
BM-40, also known as SPARC or osteonectin, is a secreted glycoprotein present in all metazoa. The protein is expressed in tissues undergoing morphogenesis, remodeling, and repair. In vitro, BM-40 binds to several collagens and is both antiproliferative and counteradhesive. Human BM-40 consists of an acidic N-terminal domain, a follistatin-like (FS) domain, and an α-helical (EC) domain that contains two functional EF-hand calcium-binding motifs. The crystal structure of the FS–EC domain pair has been determined. Calcium and collagen binding to the EC domain has been studied using site-directed mutagenesis, spectroscopy, and binding assays.
3D Structure
Schematic representation of the structure of the BM-40 FS–EC domain pair containing two calcium ions, PDB code 1BMO.35 The FS and EC domains are in green and blue respectively. Disulfide bridges are shown as yellow sticks. Calcium ions are shown as pink spheres. Made with BOBSCRIPT38 and RASTER3D.39
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