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1r5i
From Proteopedia
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'''Crystal structure of the MAM-MHC complex''' | '''Crystal structure of the MAM-MHC complex''' | ||
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[[Category: Mourad, W.]] | [[Category: Mourad, W.]] | ||
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Revision as of 04:06, 3 May 2008
Crystal structure of the MAM-MHC complex
Overview
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.
About this Structure
1R5I is a Protein complex structure of sequences from Homo sapiens and Mycoplasma arthritidis. Full crystallographic information is available from OCA.
Reference
Crystal structure of Mycoplasma arthritidis mitogen complexed with HLA-DR1 reveals a novel superantigen fold and a dimerized superantigen-MHC complex., Zhao Y, Li Z, Drozd SJ, Guo Y, Mourad W, Li H, Structure. 2004 Feb;12(2):277-88. PMID:14962388 Page seeded by OCA on Sat May 3 07:06:23 2008
Categories: Homo sapiens | Mycoplasma arthritidis | Protein complex | Drozd, S J. | Guo, Y. | Li, H. | Li, Z. | Mourad, W. | Zhao, Y. | Complex | Mam | Mhc | Superantigen
