Conformational plasticity revealed by the cocrystal structure of NKG2D and its class I MHC-like ligand ULBP3
AuthorRadaev, S; Rostro, B; Brooks, AG; Colonna, M; Sun, PD
University of Melbourne Author/sBrooks, Andrew
AffiliationMicrobiology And Immunology
Document TypeJournal Article
CitationsRadaev, S., Rostro, B., Brooks, A. G., Colonna, M. & Sun, P. D. (2001). Conformational plasticity revealed by the cocrystal structure of NKG2D and its class I MHC-like ligand ULBP3. IMMUNITY, 15 (6), pp.1039-1049. https://doi.org/10.1016/S1074-7613(01)00241-2.
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C1 - Journal Articles Refereed
NKG2D is known to trigger the natural killer (NK) cell lysis of various tumor and virally infected cells. In the NKG2D/ULBP3 complex, the structure of ULBP3 resembles the alpha1 and alpha2 domains of classical MHC molecules without a bound peptide. The lack of alpha3 and beta2m domains is compensated by replacing two hydrophobic patches at the underside of the class I MHC-like beta sheet floor with a group of hydrophilic and charged residues in ULBP3. NKG2D binds diagonally across the ULBP3 alpha helices, creating a complementary interface, an asymmetrical subunit orientation, and local conformational adjustments in the receptor. The interface is stabilized primarily by hydrogen bonds and hydrophobic interactions. Unlike the KIR receptors that recognize a conserved HLA region by a lock-and-key mechanism, NKG2D recognizes diverse ligands by an induced-fit mechanism.
KeywordsCellular Immunology; Immune System and Allergy
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