Hostname: page-component-8448b6f56d-c47g7 Total loading time: 0 Render date: 2024-04-19T04:57:04.900Z Has data issue: false hasContentIssue false

Role of DDR2 ECD Oligomerization in Binding to Collagen

Published online by Cambridge University Press:  25 July 2016

Carolyn Wang
Affiliation:
Biomedical Engineering Department, the Ohio State University Columbus, Ohio 43210, USA
David Yeung
Affiliation:
Biomedical Engineering Department, the Ohio State University Columbus, Ohio 43210, USA
Jack Wellerming
Affiliation:
Biophysics Program, the Ohio State University, Columbus, Ohio 43210, USA
Andrew Herr
Affiliation:
Department of Biochemistry and Molecular Genetics, University of Cincinnati, Cincinnati, OH, USA
Jeanette Miller
Affiliation:
Department of Biochemistry and Molecular Genetics, University of Cincinnati, Cincinnati, OH, USA
Rafael Fridman
Affiliation:
Department of Pathology, Wayne State University, Detroit, MI, USA
Gunjan Agarwal
Affiliation:
Biomedical Engineering Department, the Ohio State University Columbus, Ohio 43210, USA Biophysics Program, the Ohio State University, Columbus, Ohio 43210, USA

Abstract

Image of the first page of this content. For PDF version, please use the ‘Save PDF’ preceeding this image.'
Type
Abstract
Copyright
© Microscopy Society of America 2016 

References

References:

[1] Fu, H. L., et al, Discoidin domain receptors: unique receptor tyrosine kinases in collagen-mediated signaling. J. Biol. Chem 288 (2013). no. 11, p. 74307437.Google Scholar
[2] Vogel, W, et al, The Discoidin Domain Receptor Tyrosine Kinases Are Activated by Collagen. Mol. Cell 1 (1997). no.1, p. 1323.CrossRefGoogle ScholarPubMed
[3] Xu, H., et al, Collagen binding specificity of the discoidin domain receptors: binding sites on collagens II and III and molecular determinants for collagen IV recognition by DDR1. Matrix Biol 30 (2011). no. 1, p. 1626.Google Scholar
[4] Mihai, C. Mapping of DDR1 Distribution and Oligomerization on the Cell Surface by FRET Micrscopy. J. Miol. Biol 30 (2009). no. 2, p. 432435.Google Scholar
[5] Noordeen, N.A., et al, A transmembrane leucine zipper is required for activation of the dimeric receptor tyrosine kinase DDR1. J. Biol. Chem 281 (2006). no. 32, p. 2274422751.Google Scholar
[6] Yeung, D., et al, Oligomerization of DDR1 ECD affects receptor-ligand binding. J. Struct. Biol (2013). p. 16.Google Scholar
[7] The authors acknowledge funding from NSF CMMI award 1201111.Google Scholar