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2PTV

Structure of NK cell receptor ligand CD48

Summary for 2PTV
Entry DOI10.2210/pdb2ptv/pdb
Related2PTT
DescriptorCD48 antigen (2 entities in total)
Functional Keywordscd48, nk cell receptor, immune system
Biological sourceMus musculus (house mouse)
Cellular locationCell membrane; Lipid-anchor, GPI-anchor: P18181
Total number of polymer chains1
Total formula weight12940.73
Authors
Deng, L.,Velikovsky, C.A.,Mariuzza, R.A. (deposition date: 2007-05-08, release date: 2007-11-20, Last modification date: 2023-08-30)
Primary citationVelikovsky, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.66 Å)
Structure validation

237735

数据于2025-06-18公开中

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