3QI9

Crystal structure of mouse CD1d-alpha-phosphotidylinositol with mouse Valpha14-Vbeta6 2A3-D NKT TCR

Summary for 3QI9

• Entry DOI: 10.2210/pdb3qi9/pdb
• Descriptor: Antigen-presenting glycoprotein CD1d1, Beta-2-microglobulin, NKT TCR V alpha 14, ... (10 entities in total)
• Functional Keywords: autoreactivity, t-cell surface, immune system
• Biological source: Mus musculus (Mouse); More
• Total number of polymer chains: 4
• Total formula weight: 98324.47

Authors

Clarke, A.J.,Rossjohn, J. (deposition date: 2011-01-26, release date: 2012-02-15, Last modification date: 2023-11-01)

Primary citation

Mallevaey, T.,Clarke, A.J.,Scott-Browne, J.P.,Young, M.H.,Roisman, L.C.,Pellicci, D.G.,Patel, O.,Vivian, J.P.,Matsuda, J.L.,McCluskey, J.,Godfrey, D.I.,Marrack, P.,Rossjohn, J.,Gapin, L.
A molecular basis for NKT cell recognition of CD1d-self-antigen
Immunity, 34:315-326, 2011

PubMed Abstract: The antigen receptor for natural killer T cells (NKT TCR) binds CD1d-restricted microbial and self-lipid antigens, although the molecular basis of self-CD1d recognition is unclear. Here, we have characterized NKT TCR recognition of CD1d molecules loaded with natural self-antigens (Ags) and report the 2.3 Å resolution structure of an autoreactive NKT TCR-phosphatidylinositol-CD1d complex. NKT TCR recognition of self- and foreign antigens was underpinned by a similar mode of germline-encoded recognition of CD1d. However, NKT TCR autoreactivity is mediated by unique sequences within the non-germline-encoded CDR3β loop encoding for a hydrophobic motif that promotes self-association with CD1d. Accordingly, NKT cell autoreactivity may arise from the inherent affinity of the interaction between CD1d and the NKT TCR, resulting in the recognition of a broad range of CD1d-restricted self-antigens. This demonstrates that multiple self-antigens can be recognized in a similar manner by autoreactive NKT TCRs.

PubMed: 21376640
DOI: 10.1016/j.immuni.2011.01.013

Experimental method

X-RAY DIFFRACTION (2.3 Å)