4U7M
LRIG1 extracellular domain: Structure and Function Analysis
Summary for 4U7M
| Entry DOI | 10.2210/pdb4u7m/pdb |
| Related | 4U7L |
| Descriptor | Leucine-rich repeats and immunoglobulin-like domains protein 1, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
| Functional Keywords | stem cell marker, egfr inhibition, signaling protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 32646.73 |
| Authors | |
| Primary citation | Xu, Y.,Soo, P.,Walker, F.,Zhang, H.H.,Redpath, N.,Tan, C.W.,Nicola, N.A.,Adams, T.E.,Garrett, T.P.,Zhang, J.G.,Burgess, A.W. LRIG1 Extracellular Domain: Structure and Function Analysis. J.Mol.Biol., 427:1934-1948, 2015 Cited by PubMed 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 2.3Å 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 LRIG1-LRR-1Ig fragment to the EGF receptor (EGFR), either in solution using biosensor analysis or when the EGFR was expressed on the cell surface. The FLAG-tagged LRIG1-LRR-1Ig fragment binds weakly to colon cancer cells regardless of the presence of EGFRs. Similarly, neither the soluble LRIG1-LRR nor the LRIG1-3Ig domains nor the full-length LRIG1 co-expressed in HEK293 cells inhibited ligand-stimulated activation of cell-surface EGFR. PubMed: 25765764DOI: 10.1016/j.jmb.2015.03.001 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.757 Å) |
Structure validation
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