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Research Article

Conformation of peptides bound to the transporter associated with antigen processing (TAP)

Meike Herget, Christoph Baldauf, Christian Schölz, David Parcej, Karl-Heinz Wiesmüller, Robert Tampé, Rupert Abele, and Enrica Bordignon
PNAS first published January 4, 2011; https://doi.org/10.1073/pnas.1012355108
Meike Herget
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Christoph Baldauf
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Christian Schölz
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David Parcej
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Karl-Heinz Wiesmüller
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Robert Tampé
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Rupert Abele
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  • For correspondence: abele@em.uni-frankfurt.de enrica.bordignon@phys.chem.ethz.ch
Enrica Bordignon
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  • For correspondence: abele@em.uni-frankfurt.de enrica.bordignon@phys.chem.ethz.ch
  1. Edited by Harden M. McConnell, Stanford University, Stanford, CA, and approved December 2, 2010 (received for review August 19, 2010)

  2. ↵1M.H. and C.B. contributed equally to this work.

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Abstract

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’s position, striking differences in affinity, dynamics, and polarity were found. The side-chains’ 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.

  • adaptive immune system
  • antigenic peptide binding
  • peptide conformation
  • double electron electron resonance EPR
  • site-directed spin labeling

Footnotes

  • 2To whom correspondence may be addressed. E-mail: abele{at}em.uni-frankfurt.de or enrica.bordignon{at}phys.chem.ethz.ch.
  • Author contributions: R.T., R.A., and E.B. designed research; M.H., C.B., C.S., D.P., and E.B. performed research; C.B., D.P., K.-H.W., and R.A. contributed new reagents/analytic tools; M.H., C.B., R.T., R.A., and E.B. analyzed data; and M.H., C.B., R.T., R.A., and E.B. wrote the paper.

  • The authors declare no conflict of interest.

  • This article is a PNAS Direct Submission.

  • This article contains supporting information online at www.pnas.org/lookup/suppl/doi:10.1073/pnas.1012355108/-/DCSupplemental.

Freely available online through the PNAS open access opton.

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Conformation of peptides bound to the transporter associated with antigen processing (TAP)
Meike Herget, Christoph Baldauf, Christian Schölz, David Parcej, Karl-Heinz Wiesmüller, Robert Tampé, Rupert Abele, Enrica Bordignon
Proceedings of the National Academy of Sciences Jan 2011, DOI: 10.1073/pnas.1012355108

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Conformation of peptides bound to the transporter associated with antigen processing (TAP)
Meike Herget, Christoph Baldauf, Christian Schölz, David Parcej, Karl-Heinz Wiesmüller, Robert Tampé, Rupert Abele, Enrica Bordignon
Proceedings of the National Academy of Sciences Jan 2011, DOI: 10.1073/pnas.1012355108
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