Characterizing the N-terminal processing motif of MHC class I ligands


Most peptide ligands presented by MHC class I molecules are the product of an intracellular pathway comprising protein breakdown in the cytosol, transport into the endoplasmic reticulum, and successive N-terminal trimming events. The efficiency of each of these processes depends on the amino acid sequence of the presented ligand and its precursors. Thus, relating the amino acid composition N-terminal of presented ligands to the sequence specificity of processes in the pathway gives insight into the usage of ligand precursors in vivo. Examining the amino acid composition upstream the true N terminus of MHC class I ligands, we demonstrate the existence of a distinct N-terminal processing motif comprising approximately seven residues and matching the known preferences of proteasome and TAP, two key players in ligand processing. Furthermore, we find that some residues, which are preferred by both TAP and the proteasome, are underrepresented at positions immediately preceding the N terminus of MHC class I ligands. Based on experimentally determined aminopeptidase activities, this pattern suggests trimming next to the final N terminus to take place predominantly in the endoplasmic reticulum.


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J. Immunol.
J. Immunol. 180(5): 3210-7
23rd Feb 2008

Mark M Schatz, Björn Peters, Nadja Akkad, Nina Ullrich, Alejandra Nacarino Martinez, Oliver Carroll, Sascha Bulik, Hans-Georg Rammensee, Peter van Endert, Hermann-Georg Holzhütter, Stefan Tenzer, Hansjörg Schild

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[Elke Martinez] [Sascha Bulik] [Hermann-Georg Holzhütter]

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  • Created: 4th Jan 2013 at 11:07
  • Last updated: 24th Oct 2013 at 16:22

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