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• W2022961047 abstract "Mycoplasma arthritidis-derived mitogen (MAM) is a superantigen that can activate large fractions of T cells bearing particular TCR Vbeta elements. Here we report the crystal structure of MAM complexed with a major histocompatibility complex (MHC) antigen, HLA-DR1, loaded with haemagglutinin peptide 306-318 (HA). The structure reveals that MAM has a novel fold composed of two alpha-helical domains. This fold is entirely different from that of the pyrogenic superantigens, consisting of a beta-grasped motif and a beta barrel. In the complex, the N-terminal domain of MAM binds orthogonally to the MHC alpha1 domain and the bound HA peptide, and to a lesser extent to the MHC beta1 domain. Two MAM molecules form an asymmetric dimer and cross-link two MHC antigens to form a plausible, dimerized MAM-MHC complex. These data provide the first crystallographic evidence that superantigens can dimerize MHC molecules. Based on our structure, a model of the TCR2MAM2MHC2 complex is proposed." @default.
• W2022961047 created "2016-06-24" @default.
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• W2022961047 date "2004-02-01" @default.
• W2022961047 modified "2023-09-30" @default.
• W2022961047 title "Crystal Structure of Mycoplasma arthritidis Mitogen Complexed with HLA-DR1 Reveals a Novel Superantigen Fold and a Dimerized Superantigen-MHC Complex" @default.
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• W2022961047 doi "https://doi.org/10.1016/j.str.2004.01.008" @default.
• W2022961047 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3923524" @default.
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