PDBsum entry 4u7l

Signaling protein

PDB id: 4u7l

Contents

Protein chain

455 a.a.

Ligands

NAG-NAG

NAG ×4

Metals

_CL

Waters ×34

PDB id:

4u7l

Name:

Signaling protein

Title:

Lrig1 extracellular domain: structure and function analysis

Structure:

Leucine-rich repeats and immunoglobulin-like domains protein 1. Chain: a. Fragment: lrr repeats, residues 41-494. Synonym: lig-1. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: lrig1, lig1. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108

Resolution:

2.30Å R-factor: 0.197 R-free: 0.248

Authors:

Y.Xu

Key ref:

Y.Xu et al. (2015). LRIG1 extracellular domain: structure and function analysis. J Mol Biol, 427, 1934-1948. PubMed id: 25765764 DOI: 10.1016/j.jmb.2015.03.001

Date:

31-Jul-14 Release date: 08-Apr-15

Protein chain

Q96JA1  (LRIG1_HUMAN) -  Leucine-rich repeats and immunoglobulin-like domains protein 1 from Homo sapiens

Seq: 1093 a.a.

Struc: 455 a.a.*

* PDB and UniProt seqs differ at 6 residue positions (black crosses)

DOI no: 10.1016/j.jmb.2015.03.001

J Mol Biol 427:1934-1948 (2015)

PubMed id: 25765764

LRIG1 extracellular domain: structure and function analysis.

Y.Xu, P.Soo, F.Walker, H.H.Zhang, N.Redpath, C.W.Tan, N.A.Nicola, T.E.Adams, T.P.Garrett, J.G.Zhang, A.W.Burgess.

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.