2PTT

Structure of NK cell receptor 2B4 (CD244) bound to its ligand CD48

Summary for 2PTT

• Entry DOI: 10.2210/pdb2ptt/pdb
• Related: 2PTU 2PTV
• Descriptor: CD48 antigen, Natural killer cell receptor 2B4, SULFATE ION, ... (4 entities in total)
• Functional Keywords: 2b4, cd244, cd48, nk cell receptor, immune system
• Biological source: Mus musculus (house mouse); More
• Cellular location: Cell membrane; Lipid-anchor, GPI-anchor: P18181; Membrane; Single-pass type I membrane protein (Potential): Q07763
• Total number of polymer chains: 2
• Total formula weight: 25563.72

Authors

Deng, L.,Velikovsky, C.A.,Mariuzza, R.A. (deposition date: 2007-05-08, release date: 2007-11-20, Last modification date: 2024-11-13)

Primary citation

Velikovsky, C.A.,Deng, L.,Chlewicki, L.K.,Fernandez, M.M.,Kumar, V.,Mariuzza, R.A.
Structure of natural killer receptor 2B4 bound to CD48 reveals basis for heterophilic recognition in signaling lymphocyte activation molecule family.
Immunity, 27:572-584, 2007

PubMed Abstract: Natural killer (NK) cells eliminate virally infected and tumor cells. Among the receptors regulating NK cell function is 2B4 (CD244), a member of the signaling lymphocyte-activation molecule (SLAM) family that binds CD48. 2B4 is the only heterophilic receptor of the SLAM family, whose other members, e.g., NK-T-B-antigen (NTB-A), are self-ligands. We determined the structure of the complex between the N-terminal domains of mouse 2B4 and CD48, as well as the structures of unbound 2B4 and CD48. The complex displayed an association mode related to, yet distinct from, that of the NTB-A dimer. Binding was accompanied by the rigidification of flexible 2B4 regions containing most of the polymorphic residues across different species and receptor isoforms. We propose a model for 2B4-CD48 interactions that permits the intermixing of SLAM receptors with major histocompatibility complex-specific receptors in the NK cell immune synapse. This analysis revealed the basis for heterophilic recognition within the SLAM family.

PubMed: 17950006
DOI: 10.1016/j.immuni.2007.08.019

Experimental method

X-RAY DIFFRACTION (1.63 Å)