2OJE

Mycoplasma arthritidis-derived mitogen complexed with class II MHC molecule HLA-DR1/HA complex in the presence of EDTA

Summary for 2OJE

• Entry DOI: 10.2210/pdb2oje/pdb
• Related: 1R5I
• Descriptor: HLA class II histocompatibility antigen, DR alpha chain precursor, HLA class II histocompatibility antigen, DRB1-1 beta chain precursor, haemagglutinin peptide 306-318, ... (6 entities in total)
• Functional Keywords: superantigen, mhc, immune system
• Biological source: Homo sapiens (human); More
• Cellular location: Cell membrane; Single-pass type I membrane protein: P01903 P04229
• Total number of polymer chains: 8
• Total formula weight: 140618.34

Authors

Li, H.,Zhao, Y.,Guo, Y.,Li, Z.,Eisele, L.,Mourad, W. (deposition date: 2007-01-12, release date: 2007-01-23, Last modification date: 2024-10-16)

Primary citation

Li, H.,Zhao, Y.,Guo, Y.,Li, Z.,Eisele, L.,Mourad, W.
Zinc induces dimerization of the class II major histocompatibility complex molecule that leads to cooperative binding to a superantigen.
J.Biol.Chem., 282:5991-6000, 2007

PubMed Abstract: Dimerization of class II major histocompatibility complex (MHC) plays an important role in the MHC biological function. Mycoplasma arthritidis-derived mitogen (MAM) is a superantigen that can activate large fractions of T cells bearing specific T cell receptor Vbeta elements. Here we have used structural, sedimentation, and surface plasmon resonance detection approaches to investigate the molecular interactions between MAM and the class II MHC molecule HLA-DR1 in the context of a hemagglutinin peptide-(306-318) (HA). Our results revealed that zinc ion can efficiently induce the dimerization of the HLA-DR1/HA complex. Because the crystal structure of the MAM/HLA-DR1/hemagglutinin complex in the presence of EDTA is nearly identical to the structure of the complex crystallized in the presence of zinc ion, Zn(2+) is evidently not directly involved in the binding between MAM and HLA-DR1. Sedimentation and surface plasmon resonance studies further revealed that MAM binds the HLA-DR1/HA complex with high affinity in a 1:1 stoichiometry, in the absence of Zn(2+). However, in the presence of Zn(2+), a dimerized MAM/HLA-DR1/HA complex can arise through the Zn(2+)-induced DR1 dimer. In the presence of Zn(2+), cooperative binding of MAM to the DR1 dimer was also observed.

PubMed: 17166841
DOI: 10.1074/jbc.M608482200

Experimental method

X-RAY DIFFRACTION (3 Å)