2WBJ
TCR complex
Summary for 2WBJ
Entry DOI | 10.2210/pdb2wbj/pdb |
Related | 1A6A 1AQD 1BX2 1D5M 1D5X 1D5Z 1D6E 1DLH 1FV1 1FYT 1H15 1HQR 1HXY 1J8H 1JWM 1JWS 1JWU 1KG0 1KLG 1KLU 1LO5 1SEB 1SJE 1SJH 1T5W 1T5X 1YMM 1ZGL 2G9H 2SEB |
Descriptor | HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN, HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DRB1-15 BETA CHAIN, OB TCR, ... (7 entities in total) |
Functional Keywords | transmembrane, immune response, t cell receptor, mhc ii, membrane, receptor, molecular mimicry, multiple sclerosis, immune system, autoimmunity, glycoprotein, mhc class ii |
Biological source | HOMO SAPIENS (HUMAN) More |
Total number of polymer chains | 8 |
Total formula weight | 203970.30 |
Authors | Harkiolaki, M.,Holmes, S.L.,Svendsen, P.,Gregersen, J.W.,Jensen, L.T.,McMahon, R.,Friese, M.A.,van Boxel, G.,Etzensperger, R.,Tzartos, J.S.,Kranc, K.,Sainsbury, S.,Harlos, K.,Mellins, E.D.,Palace, J.,Esiri, M.M.,van der Merwe, P.A.,Jones, E.Y.,Fugger, L. (deposition date: 2009-03-02, release date: 2009-04-07, Last modification date: 2024-11-13) |
Primary citation | Harkiolaki, M.,Holmes, S.L.,Svendsen, P.,Gregersen, J.W.,Jensen, L.T.,Mcmahon, R.,Friese, M.A.,Van Boxel, G.,Etzensperger, R.,Tzartos, J.S.,Kranc, K.,Sainsbury, S.,Harlos, K.,Mellins, E.D.,Palace, J.,Esiri, M.M.,Van Der Merwe, P.A.,Jones, E.Y.,Fugger, L. T Cell-Mediated Autoimmune Disease due to Low-Affinity Crossreactivity to Common Microbial Peptides. Immunity, 30:348-, 2009 Cited by PubMed Abstract: Environmental factors account for 75% of the risk of developing multiple sclerosis (MS). Numerous infections have been suspected as environmental disease triggers, but none of them has consistently been incriminated, and it is unclear how so many different infections may play a role. We show that a microbial peptide, common to several major classes of bacteria, can induce MS-like disease in humanized mice by crossreacting with a T cell receptor (TCR) that also recognizes a peptide from myelin basic protein, a candidate MS autoantigen. Structural analysis demonstrates this crossreactivity is due to structural mimicry of a binding hotspot shared by self and microbial antigens, rather than to degenerate TCR recognition. Biophysical studies reveal that the autoreactive TCR binding affinity is markedly lower for the microbial (mimicry) peptide than for the autoantigenic peptide. Thus, these data suggest a possible explanation for the difficulty in incriminating individual infections in the development of MS. PubMed: 19303388DOI: 10.1016/J.IMMUNI.2009.01.009 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
Download full validation report
