Title :
LRIG1 extracellular
domain : structure and function analysis
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-1 Ig 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
Output (sent_index, trigger,
protein,
sugar,
site):
- 1. LRIG1-ECD, , LRIG1, the LRIG1-LRR (leucine-rich repeat) domain, -
- 1. leucine-rich, , -, leucine-rich repeat, leucine
- 1. leucine-rich, , -, the LRIG1-LRR (leucine-rich repeat) domain, leucine
Output(Part-Of) (sent_index,
protein,
site):
- 0. LRIG1, domain
- 1. LRIG1, domain
- 1. LRIG1, fragment
- 1. LRIG1, fragments
- 2. LRIG1, domains
- 4. LRIG1, domain
- 4. LRIG1, fragment
- 5. LRIG1, domains
- 5. LRIG1, fragment
- 6. FLAG-tagged LRIG1, fragment
- 7. LRIG1, domains
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):