{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,10]],"date-time":"2026-06-10T16:31:30Z","timestamp":1781109090432,"version":"3.54.1"},"reference-count":28,"publisher":"National Academy of Sciences","issue":"4","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2011,1,25]]},"abstract":"<jats:p>The ATP-binding cassette transporter associated with antigen processing (TAP) plays a key role in the adaptive immune defense against infected or malignantly transformed cells by translocating proteasomal degradation products into the lumen of the endoplasmic reticulum for loading onto MHC class I molecules. The broad substrate spectrum of TAP, rendering peptides from 8 to 40 residues, including even branched or modified molecules, suggests an unforeseen structural flexibility of the substrate-binding pocket. Here we used EPR spectroscopy to reveal conformational details of the bound peptides. Side-chain dynamics and environmental polarity were derived from covalently attached 2,2,5,5-tetramethylpyrrolidine-1-oxyl spin probes, whereas 2,2,6,6-tetramethylpiperidine-1-oxyl-4-amino-4-carboxylic acid spin-labeled peptides were used to detect backbone properties. Dependent on the spin probe\u2019s position, striking differences in affinity, dynamics, and polarity were found. The side-chains\u2019 mobility was strongly restricted at the ends of the peptide, whereas the central region was flexible, suggesting a central peptide bulge. In the end, double electron electron resonance allowed the determination of intrapeptide distances in doubly labeled peptides bound to TAP. Simulations based on a rotamer library led to the conclusion that peptides bind to TAP in an extended kinked structure, analogous to those bound to MHC class I proteins.<\/jats:p>","DOI":"10.1073\/pnas.1012355108","type":"journal-article","created":{"date-parts":[[2011,1,4]],"date-time":"2011-01-04T20:45:06Z","timestamp":1294173906000},"page":"1349-1354","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":44,"title":["Conformation of peptides bound to the transporter associated with antigen processing (TAP)"],"prefix":"10.1073","volume":"108","author":[{"given":"Meike","family":"Herget","sequence":"first","affiliation":[{"name":"Institute of Biochemistry, Goethe-University Frankfurt, Max-von-Laue Strasse 9, 60438 Frankfurt am Main, Germany;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christoph","family":"Baldauf","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry, Goethe-University Frankfurt, Max-von-Laue Strasse 9, 60438 Frankfurt am Main, Germany;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christian","family":"Sch\u00f6lz","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry, Goethe-University Frankfurt, Max-von-Laue Strasse 9, 60438 Frankfurt am Main, Germany;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David","family":"Parcej","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry, Goethe-University Frankfurt, Max-von-Laue Strasse 9, 60438 Frankfurt am Main, Germany;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karl-Heinz","family":"Wiesm\u00fcller","sequence":"additional","affiliation":[{"name":"EMC Microcollections GmbH, Sindelfinger Strasse 3, 72070 T\u00fcbingen, Germany; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert","family":"Tamp\u00e9","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry, Goethe-University Frankfurt, Max-von-Laue Strasse 9, 60438 Frankfurt am Main, Germany;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rupert","family":"Abele","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry, Goethe-University Frankfurt, Max-von-Laue Strasse 9, 60438 Frankfurt am Main, Germany;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Enrica","family":"Bordignon","sequence":"additional","affiliation":[{"name":"Eidgen\u00f6ssiche Technische Hochschule Zurich, Laboratory for Physical Chemistry, Wolfgang-Pauli-Strasse 10, 8093 Zurich, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2011,1,4]]},"reference":[{"key":"e_1_3_3_1_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.0105-2896.2005.00316.x"},{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0959-440X(02)00399-8"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.sbi.2007.07.003"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M312816200"},{"key":"e_1_3_3_5_2","doi-asserted-by":"crossref","first-page":"5467","DOI":"10.4049\/jimmunol.157.12.5467","article-title":"Multiple regions of the transporter associated with antigen processing (TAP) contribute to its peptide binding site","volume":"157","author":"Nijenhuis M","year":"1996","unstructured":"M Nijenhuis, GJ Hammerling, Multiple regions of the transporter associated with antigen processing (TAP) contribute to its peptide binding site. 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