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Methyl-Labeling Assisted NMR Structure Determination of a 66 KDA Growth Factor-Receptor Complex

Authors :
Morkos A. Henen
Ravindra Kodali
Cynthia S. Hinck
Christian W Zwieb
Andrew P. Hinck
Source :
Biophysical Journal. 112:487a-488a
Publication Year :
2017
Publisher :
Elsevier BV, 2017.

Abstract

TGF-β1, TGF- β2, and TGF-β3 are 26 kDa disulfide-linked homodimeric signaling proteins. They all signal through the TGF-β type I and type II receptors, yet TGF-β2, which is well known to bind TβRII several-hundred fold more weakly than TGF-β1 and TGF-β3, has an additional requirement for the TGF-β type III receptor (TβRIII), a membrane-anchored non-signaling receptor that potentiates the binding of TβRII. Though it is known that TβRIII has two component domains that bind TGF-β2 non-cooperatively at independent sites, the structure of these domains bound to TGF-β2 and residues responsible for specific binding are not yet known.

Details

ISSN :
00063495
Volume :
112
Database :
OpenAIRE
Journal :
Biophysical Journal
Accession number :
edsair.doi...........9e53ad4ade4f6ee97685ac235f52b2e2
Full Text :
https://doi.org/10.1016/j.bpj.2016.11.2638