4H5S

Complex structure of Necl-2 and CRTAM

4H5S の概要

• エントリーDOI: 10.2210/pdb4h5s/pdb
• 分子名称: Cytotoxic and regulatory T-cell molecule, Cell adhesion molecule 1 (3 entities in total)
• 機能のキーワード: ig fold, cell adhesion, immune recognition
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Membrane; Single-pass type I membrane protein (Potential): O95727; Cell membrane; Single-pass type I membrane protein: Q9BY67
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 22874.85

構造登録者

Zhang, S.,Lu, G.,Qi, J.,Li, Y.,Zhang, Z.,Zhang, B.,Yan, J.,Gao, G.F. (登録日: 2012-09-18, 公開日: 2013-08-07, 最終更新日: 2024-11-20)

主引用文献

Zhang, S.,Lu, G.,Qi, J.,Li, Y.,Zhang, Z.,Zhang, B.,Fan, Z.,Yan, J.,Gao, G.F.
Competition of cell adhesion and immune recognition: insights into the interaction between CRTAM and nectin-like 2.
Structure, 21:1430-1439, 2013

PubMed Abstract: Nectin and nectin-like proteins are cell adhesion molecules that mediate the formation of cell adherens junctions by forming homo- or heterodimers. Some members of this protein family can also be used by immune receptors to mediate immune recognition. For instance, nectin-like 2 (Necl-2) is used as a ligand for the immune system by interaction with the immune receptor CRTAM (class-I MHC-restricted T cell associated molecule), which is mainly expressed on the surface of cytotoxic lymphocyte cells. However, the Necl-2/CRTAM binding mode and its relationship to cell adhesion are not known. Here, we report a Necl-2/CRTAM complex structure, demonstrating that Necl-2 binding to CRTAM competes with the dimerization of CRTAM and possibly Necl-2. Necl-2 occupies the CRTAM homodimer interface, making homodimerization impossible. Mutational and functional analyses identified key amino acids (double "lock-and-key") responsible for the binding. Our work illustrates how the cell adhesion molecule Necl-2 competitively binds the immune receptor CRTAM.

PubMed: 23871486
DOI: 10.1016/j.str.2013.06.006

実験手法

X-RAY DIFFRACTION (1.7 Å)