5WER

Crystal Structure of TAPBPR and H2-Dd complex

Summary for 5WER

• Entry DOI: 10.2210/pdb5wer/pdb
• Related: 5MES
• Descriptor: H-2 class I histocompatibility antigen, D-D alpha chain, Beta-2-microglobulin, TAP binding protein related, ... (7 entities in total)
• Functional Keywords: antigen presentation, peptide editing, major histompatibility complex class i, mhc-i, tapasin, peptide loading complex, plc, immune response, immune system
• Biological source: Mus musculus (Mouse); More
• Total number of polymer chains: 12
• Total formula weight: 346591.12

Authors

Jiang, J.S.,Natarajan, K.,Boyd, L.F.,Margulies, D.H. (deposition date: 2017-07-10, release date: 2017-10-18, Last modification date: 2024-12-25)

Primary citation

Jiang, J.,Natarajan, K.,Boyd, L.F.,Morozov, G.I.,Mage, M.G.,Margulies, D.H.
Crystal structure of a TAPBPR-MHC I complex reveals the mechanism of peptide editing in antigen presentation.
Science, 358:1064-1068, 2017

PubMed Abstract: Central to CD8 T cell-mediated immunity is the recognition of peptide-major histocompatibility complex class I (p-MHC I) proteins displayed by antigen-presenting cells. Chaperone-mediated loading of high-affinity peptides onto MHC I is a key step in the MHC I antigen presentation pathway. However, the structure of MHC I with a chaperone that facilitates peptide loading has not been determined. We report the crystal structure of MHC I in complex with the peptide editor TAPBPR (TAP-binding protein-related), a tapasin homolog. TAPBPR remodels the peptide-binding groove of MHC I, resulting in the release of low-affinity peptide. Changes include groove relaxation, modifications of key binding pockets, and domain adjustments. This structure captures a peptide-receptive state of MHC I and provides insights into the mechanism of peptide editing by TAPBPR and, by analogy, tapasin.

PubMed: 29025991
DOI: 10.1126/science.aao5154

Experimental method

X-RAY DIFFRACTION (3.412 Å)