http://purl.uniprot.org/citations/19429706 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/19429706 | http://www.w3.org/2000/01/rdf-schema#comment | "The bone morphogenetic protein (BMP)-1/tolloid metalloproteinases are evolutionarily conserved enzymes that are fundamental to dorsal-ventral patterning and tissue morphogenesis. The lack of knowledge regarding how these proteinases recognize and cleave their substrates represents a major hurdle to understanding tissue assembly and embryonic patterning. Although BMP-1 and mammalian tolloid (mTLD) are splice variants, it is puzzling why BMP-1, which lacks 3 of the 7 noncatalytic domains present in all other family members, is the most effective proteinase. Using a combination of single-particle electron microscopy, small-angle X-ray scattering, and other biophysical measurements in solution, we show that mTLD, but not BMP-1, forms a calcium-ion-dependent dimer under physiological conditions. Using a domain deletion approach, we provide evidence that EGF2, which is absent in BMP-1, is critical to the formation of the dimer. Based on a combination of structural and functional data, we propose that mTLD activity is regulated by a substrate exclusion mechanism. These results provide a mechanistic insight into how alternative splicing of the Bmp1 gene produces 2 proteinases with differing biological activities and have broad implications for regulation of BMP-1/mTLD and related proteinases during BMP signaling and tissue assembly."xsd:string |
http://purl.uniprot.org/citations/19429706 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.0812178106"xsd:string |
http://purl.uniprot.org/citations/19429706 | http://purl.uniprot.org/core/author | "Grossmann J.G."xsd:string |
http://purl.uniprot.org/citations/19429706 | http://purl.uniprot.org/core/author | "Kammerer R.A."xsd:string |
http://purl.uniprot.org/citations/19429706 | http://purl.uniprot.org/core/author | "Baldock C."xsd:string |
http://purl.uniprot.org/citations/19429706 | http://purl.uniprot.org/core/author | "Jowitt T.A."xsd:string |
http://purl.uniprot.org/citations/19429706 | http://purl.uniprot.org/core/author | "Berry R."xsd:string |
http://purl.uniprot.org/citations/19429706 | http://purl.uniprot.org/core/author | "Kadler K.E."xsd:string |
http://purl.uniprot.org/citations/19429706 | http://purl.uniprot.org/core/author | "Roessle M."xsd:string |
http://purl.uniprot.org/citations/19429706 | http://purl.uniprot.org/core/author | "Ferrand J."xsd:string |
http://purl.uniprot.org/citations/19429706 | http://purl.uniprot.org/core/author | "Canty-Laird E.G."xsd:string |
http://purl.uniprot.org/citations/19429706 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
http://purl.uniprot.org/citations/19429706 | http://purl.uniprot.org/core/name | "Proc Natl Acad Sci U S A"xsd:string |
http://purl.uniprot.org/citations/19429706 | http://purl.uniprot.org/core/pages | "8561-8566"xsd:string |
http://purl.uniprot.org/citations/19429706 | http://purl.uniprot.org/core/title | "Role of dimerization and substrate exclusion in the regulation of bone morphogenetic protein-1 and mammalian tolloid."xsd:string |
http://purl.uniprot.org/citations/19429706 | http://purl.uniprot.org/core/volume | "106"xsd:string |
http://purl.uniprot.org/citations/19429706 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/19429706 |
http://purl.uniprot.org/citations/19429706 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/19429706 |
http://purl.uniprot.org/uniprot/P13497#attribution-6A1FAE28FF80925DA230187953D9CC18 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/19429706 |