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Betaglycan has two independent domains required for high affinity TGF-β binding: proteolytic cleavage separates the domains and inactivates the neutralizing activity of the soluble receptor
Betaglycan is a co-receptor for members of the TGF-β superfamily. Mutagenesis has identified two ligand binding regions, one at the membrane-distal and the other at the membrane-proximal half of the betaglycan ectodomain. Here we show that partial plasmin digestion of soluble betaglycan produces two...
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| Hlavní autoři: | , , , , , , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
2009
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2796082/ https://ncbi.nlm.nih.gov/pubmed/19842711 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi901528w |
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