Structural mechanism of tapasin-mediated MHC-I peptide loading in antigen presentation
Jiansheng Jiang,
Daniel K. Taylor,
Ellen J. Kim,
Lisa F. Boyd,
Javeed Ahmad,
Michael G. Mage,
Hau V. Truong,
Claire H. Woodward,
Nikolaos G. Sgourakis,
Peter Cresswell,
David H. Margulies (dmargulies@niaid.nih.gov) and
Kannan Natarajan (knatarajan@niaid.nih.gov)
Additional contact information
Jiansheng Jiang: National Institutes of Health
Daniel K. Taylor: National Institutes of Health
Ellen J. Kim: National Institutes of Health
Lisa F. Boyd: National Institutes of Health
Javeed Ahmad: National Institutes of Health
Michael G. Mage: National Institutes of Health
Hau V. Truong: University of Pennsylvania
Claire H. Woodward: University of Pennsylvania
Nikolaos G. Sgourakis: University of Pennsylvania
Peter Cresswell: Yale University School of Medicine
David H. Margulies: National Institutes of Health
Kannan Natarajan: National Institutes of Health
Nature Communications, 2022, vol. 13, issue 1, 1-13
Abstract:
Abstract Loading of MHC-I molecules with peptide by the catalytic chaperone tapasin in the peptide loading complex plays a critical role in antigen presentation and immune recognition. Mechanistic insight has been hampered by the lack of detailed structural information concerning tapasin–MHC-I. We present here crystal structures of human tapasin complexed with the MHC-I molecule HLA-B*44:05, and with each of two anti-tapasin antibodies. The tapasin-stabilized peptide-receptive state of HLA-B*44:05 is characterized by distortion of the peptide binding groove and destabilization of the β2-microglobulin interaction, leading to release of peptide. Movements of the membrane proximal Ig-like domains of tapasin, HLA-B*44:05, and β2-microglobulin accompany the transition to a peptide-receptive state. Together this ensemble of crystal structures provides insights into a distinct mechanism of tapasin-mediated peptide exchange.
Date: 2022
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-33153-8
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DOI: 10.1038/s41467-022-33153-8
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