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PDBsum entry 2ptv
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Immune system
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PDB id
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2ptv
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References listed in PDB file
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Key reference
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Title
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Structure of natural killer receptor 2b4 bound to cd48 reveals basis for heterophilic recognition in signaling lymphocyte activation molecule family.
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Authors
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C.A.Velikovsky,
L.Deng,
L.K.Chlewicki,
M.M.Fernández,
V.Kumar,
R.A.Mariuzza.
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Ref.
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Immunity, 2007,
27,
572-584.
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PubMed id
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Abstract
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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.
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