{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T23:17:56Z","timestamp":1791328676605,"version":"4.3.1"},"reference-count":44,"publisher":"American Association for the Advancement of Science (AAAS)","issue":"5192","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Science"],"published-print":{"date-parts":[[1994,12,16]]},"abstract":"<jats:p>\n                    The three-dimensional structure of a\n                    <jats:italic>Staphylococcus aureus<\/jats:italic>\n                    superantigen, toxic shock syndrome toxin-1 (TSST-1), complexed with a human class II major histocompatibility molecule (DR1), was determined by x-ray crystallography. The TSST-1 binding site on DR1 overlaps that of the superantigen\n                    <jats:italic>S. aureus<\/jats:italic>\n                    enterotoxin B (SEB), but the two binding modes differ. Whereas SEB binds primarily off one edge of the peptide binding site of DR1, TSST-1 extends over almost one-half of the binding site and contacts both the flanking \u03b1 helices of the histocompatibility antigen and the bound peptide. This difference suggests that the T cell receptor (TCR) would bind to TSST-1:DR1 very differently than to DR1:peptide or SEB:DR1. It also suggests that TSST-1 binding may be dependent on the peptide, though less so than TCR binding, providing a possible explanation for the inability of TSST-1 to competitively block SEB binding to all DR1 molecules on cells (even though the binding sites of TSST-1 and SEB on DR1 overlap almost completely) and suggesting the possibility that T cell activation by superantigen could be directed by peptide antigen.\n                  <\/jats:p>","DOI":"10.1126\/science.7997880","type":"journal-article","created":{"date-parts":[[2006,10,5]],"date-time":"2006-10-05T20:01:25Z","timestamp":1160078485000},"page":"1870-1874","source":"Crossref","is-referenced-by-count":231,"title":["Toxic Shock Syndrome Toxin-1 Complexed with a Class II Major Histocompatibility Molecule HLA-DR1"],"prefix":"10.1126","volume":"266","author":[{"given":"Jongsun","family":"Kim","sequence":"first","affiliation":[{"name":"Howard Hughes Medical Institute and Laboratory of Molecular Medicine, Children's Hospital, Boston, MA 02115, USA"},{"name":"Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert G.","family":"Urban","sequence":"additional","affiliation":[{"name":"Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jack L.","family":"Strominger","sequence":"additional","affiliation":[{"name":"Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Don C.","family":"Wiley","sequence":"additional","affiliation":[{"name":"Howard Hughes Medical Institute and Laboratory of Molecular Medicine, Children's Hospital, Boston, MA 02115, USA"},{"name":"Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"221","reference":[{"key":"e_1_2_1_1_1","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1038\/367094a0","volume":"367","year":"1994","unstructured":"ACHARYA, K.R., STRUCTURAL BASIS OF SUPERANTIGEN ACTION INFERRED FROM CRYSTAL-STRUCTURE OF TOXIC-SHOCK SYNDROME TOXIN-1, NATURE 367: 94 (1994).","journal-title":"NATURE"},{"key":"e_1_2_1_2_1","first-page":"215","volume":"17","year":"1984","unstructured":"BETHGE, P. 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