LRIG1 extracellular domain: Structure and function analysis

Y Xu; P Soo; F Walker; HH Zhang; N Redpath; CW Tan; NA Nicola; TE Adams; TP Garrett; JG Zhang; AW Burgess

Journal article

LRIG1 extracellular domain: Structure and function analysis

Y Xu, P Soo, F Walker, HH Zhang, N Redpath, CW Tan, NA Nicola, TE Adams, TP Garrett, JG Zhang, AW Burgess

Journal of Molecular Biology | ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD | Published : 2015

DOI: 10.1016/j.jmb.2015.03.001

Abstract

We have expressed and purified three soluble fragments of the human LRIG1-ECD (extracellular domain): the LRIG1-LRR (leucine-rich repeat) domain, the LRIG1-3Ig (immunoglobulin-like) domain, and the LRIG1-LRR-1Ig fragment using baculovirus vectors in insect cells. The two LRIG1 domains crystallised so that we have been able to determine the three-dimensional structures at 2.3 Å resolution. We developed a three-dimensional structure for the LRIG1-ECD using homology modelling based on the LINGO-1 structure. The LRIG1-LRR domain and the LRIG1-LRR-1Ig fragment are monomers in solution, whereas the LRIG1-3Ig domain appears to be dimeric. We could not detect any binding of the LRIG1 domains or the ..

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University of Melbourne Researchers

Nicos Nicola Author

Chin Tan Author

Antony Burgess Author

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Grants

Awarded by National Science Foundation

Funding Acknowledgements

We thank P. M. Colman and M. Lawrence for structural insight and continual support. This work was supported in part by funding from the National Health and Medical Research Council under Programme Grants 487922 and 1016647 and Project Grant 1004945. The Ludwig Institute for Cancer Research provided funding for part of this project. This work was made possible through Victorian State Government Operational Infrastructure Support and Australian Government National Health and Medical Research Council Independent Research Institute Infrastructure Support Scheme.