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  Requirements for peptide binding to the human transporter associated with antigen processing revealed by peptide scans and complex peptide libraries

Uebel, S., Meyer, T. H., Kraas, W., Kienle, S., Jung, G., Wiesmüller, K. H., et al. (1995). Requirements for peptide binding to the human transporter associated with antigen processing revealed by peptide scans and complex peptide libraries. Journal of Biological Chemistry, 270(31), 18512-18516.

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Uebel, S.1, Author              
Meyer, T. H., Author
Kraas, W., Author
Kienle, S., Author
Jung, G., Author
Wiesmüller, K. H., Author
Tampe, R., Author
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1External Organizations, ou_persistent22              

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Free keywords: Major histocompatibility complex; Class-i molecules; Translocation; Mhc.; Biochemistry & biophysics.
 Abstract: Antigenic peptides are translocated into the lumen of the endoplasmic reticulum by the action of the transporter associated with antigen processing (TAP), where they are subsequently needed for the correct assembly of major histocompatability complex molecules. The transport function was reconstituted in insect cells by expression of both TAP genes. On the basis of this overexpression system, substrate selection was analyzed in detail by a direct bimolecular peptide binding assay. Competition assays with peptide variants, including substitutions of residues with alanine or structurally related amino acids, underline the broad peptide specificity of the human TAP complex. Steric requirements of the substrate-binding pocket were mapped using elongated peptides and scans with bulky, hydrophobic amino acids. Complex nonapeptide libraries were used to determine the contribution of each residue to stabilize peptide-TAP complexes. For the first time, this ap proach lets us directly evaluate the importance of peptide selection for the overall process of antigen presentation on the level of the peptide transporter. [References: 25]

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 Dates: 1995-08-04
 Publication Status: Published in print
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 Identifiers: eDoc: 318378
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Title: Journal of Biological Chemistry
Source Genre: Journal
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Pages: - Volume / Issue: 270 (31) Sequence Number: - Start / End Page: 18512 - 18516 Identifier: -