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dc.contributor.authorBalaji, GR
dc.contributor.authorAguilar, OA
dc.contributor.authorTanaka, M
dc.contributor.authorShingu-Vazquez, MA
dc.contributor.authorFu, Z
dc.contributor.authorGully, BS
dc.contributor.authorLanier, LL
dc.contributor.authorCarlyle, JR
dc.contributor.authorRossjohn, J
dc.contributor.authorBerry, R
dc.date.accessioned2020-12-09T23:30:16Z
dc.date.available2020-12-09T23:30:16Z
dc.date.issued2018-11-05
dc.identifierpii: 10.1038/s41467-018-06989-2
dc.identifier.citationBalaji, G. R., Aguilar, O. A., Tanaka, M., Shingu-Vazquez, M. A., Fu, Z., Gully, B. S., Lanier, L. L., Carlyle, J. R., Rossjohn, J. & Berry, R. (2018). Recognition of host Clr-b by the inhibitory NKR-P1B receptor provides a basis for missing-self recognition. NATURE COMMUNICATIONS, 9 (1), https://doi.org/10.1038/s41467-018-06989-2.
dc.identifier.issn2041-1723
dc.identifier.urihttp://hdl.handle.net/11343/253243
dc.description.abstractThe interaction between natural killer (NK) cell inhibitory receptors and their cognate ligands constitutes a key mechanism by which healthy tissues are protected from NK cell-mediated lysis. However, self-ligand recognition remains poorly understood within the prototypical NKR-P1 receptor family. Here we report the structure of the inhibitory NKR-P1B receptor bound to its cognate host ligand, Clr-b. NKR-P1B and Clr-b interact via a head-to-head docking mode through an interface that includes a large array of polar interactions. NKR-P1B:Clr-b recognition is extremely sensitive to mutations at the heterodimeric interface, with most mutations severely impacting both Clr-b binding and NKR-P1B receptor function to implicate a low affinity interaction. Within the structure, two NKR-P1B:Clr-b complexes are cross-linked by a non-classic NKR-P1B homodimer, and the disruption of homodimer formation abrogates Clr-b recognition. These data provide an insight into a fundamental missing-self recognition system and suggest an avidity-based mechanism underpins NKR-P1B receptor function.
dc.languageEnglish
dc.publisherNATURE PUBLISHING GROUP
dc.rights.urihttps://creativecommons.org/licenses/by/4.0
dc.titleRecognition of host Clr-b by the inhibitory NKR-P1B receptor provides a basis for missing-self recognition
dc.typeJournal Article
dc.identifier.doi10.1038/s41467-018-06989-2
melbourne.affiliation.departmentMicrobiology and Immunology
melbourne.source.titleNature Communications
melbourne.source.volume9
melbourne.source.issue1
dc.rights.licenseCC BY
melbourne.elementsid1355541
melbourne.contributor.authorRossjohn, Jamie
dc.identifier.eissn2041-1723
melbourne.accessrightsOpen Access


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