{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,10]],"date-time":"2026-02-10T08:57:02Z","timestamp":1770713822027,"version":"3.49.0"},"reference-count":17,"publisher":"Wiley","issue":"9","license":[{"start":{"date-parts":[[2005,12,7]],"date-time":"2005-12-07T00:00:00Z","timestamp":1133913600000},"content-version":"vor","delay-in-days":4845,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Eur J Immunol"],"published-print":{"date-parts":[[1992,9]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The peptides presented by major histocompatibility complex class I molecules adhere to strict rules concerning peptide length and occupancy by certain amino acid residues at anchor positions. Peptides presented by HLA\u2010A*0201 molecules, for example, are generally nonapeptides requiring Leu or Met at position 2 and an aliphatic residue, predominantly Val, at position 9. A closely related molecule, HLA\u2010A*0205, differing from the former at four amino acid residues, has a related but substantially different peptide motif. A*0205\u2010presented peptides are still nonapeptides, and position 9 is still aliphatic, although it is preferentially occupied by Leu instead of Val. Position 2 not only allows aliphatic residues but also polar ones. Occupancy at position 6, considered as an auxiliary anchor in A*0201, as well as non\u2010anchor residues at positions 3, 4, and 8 are relatively well conserved between the two peptide motifs. Thus, although a number of the T cell epitopes presented by the two HLA\u2010A2 forms is expected to be identical, a considerable number of epitopes should be different.<\/jats:p>","DOI":"10.1002\/eji.1830220940","type":"journal-article","created":{"date-parts":[[2007,3,1]],"date-time":"2007-03-01T17:49:44Z","timestamp":1172771384000},"page":"2453-2456","source":"Crossref","is-referenced-by-count":57,"title":["Peptide motifs of closely related HLA class I molecules encompass substantial differences"],"prefix":"10.1002","volume":"22","author":[{"given":"Olaf","family":"R\u00f6tzschke","sequence":"first","affiliation":[]},{"given":"Kirsten","family":"Falk","sequence":"additional","affiliation":[]},{"given":"Stefan","family":"Stevanovi\u0107","sequence":"additional","affiliation":[]},{"given":"G\u00fcnther","family":"Jung","sequence":"additional","affiliation":[]},{"given":"Hans\u2010Georg","family":"Rammensee","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2005,12,7]]},"reference":[{"key":"e_1_2_1_2_2","doi-asserted-by":"publisher","DOI":"10.1038\/248701a0"},{"key":"e_1_2_1_3_2","doi-asserted-by":"crossref","first-page":"2194","DOI":"10.4049\/jimmunol.133.4.2194","volume":"133","author":"Wabuke\u2010Bunoti M. 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R\u00f6tzschke O. Rognan D. Folkers G. Rammensee H.\u2010G.andJung G. Angew. 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