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TitleThe TbetaR-I Pre-Helix Extension Is Structurally Ordered in the Unbound Form and Its Flanking Prolines Are Essential for Binding
Journal, issue, pagesJ. Mol. Biol., Vol. 412, Page 601-618, Year 2011
Publish dateNov 4, 2010 (structure data deposition date)
AuthorsZuniga, J.E. / Ilangovan, U. / Mahlawat, P. / Hinck, C.S. / Huang, T. / Groppe, J.C. / McEwen, D.G. / Hinck, A.P.
External linksJ. Mol. Biol. / PubMed:21821041
MethodsNMR (solution)
Structure data

PDB-2l5s:
Solution structure of the extracellular domain of the TGF-beta type I receptor
Method: SOLUTION NMR

Source
  • homo sapiens (human)
KeywordsSIGNALING PROTEIN / ALK5 / transforming growth factor beta / type I receptor

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