4U7M

LRIG1 extracellular domain: Structure and Function Analysis

4U7M の概要

• エントリーDOI: 10.2210/pdb4u7m/pdb
• 関連するPDBエントリー: 4U7L
• 分子名称: Leucine-rich repeats and immunoglobulin-like domains protein 1, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: stem cell marker, egfr inhibition, signaling protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32646.73

構造登録者

Xu, Y. (登録日: 2014-07-31, 公開日: 2015-04-08, 最終更新日: 2024-10-23)

主引用文献

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

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: 25765764
DOI: 10.1016/j.jmb.2015.03.001

実験手法

X-RAY DIFFRACTION (2.757 Å)