7TUE
Crystal structure of Tapasin in complex with HLA-B*44:05 (T73C)
Summary for 7TUE
| Entry DOI | 10.2210/pdb7tue/pdb |
| Related | 7TUC 7TUD 7TUF 7TUG 7TUH |
| Descriptor | HLA class I histocompatibility antigen, B alpha chain, Tapasin, Beta-2-microglobulin (3 entities in total) |
| Functional Keywords | tapasin, histocompatibility complex class i, mhc-i, hla, peptide editing, peptide loading complex, plc, antigen presentation, immune response, immune system |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 3 |
| Total formula weight | 88423.15 |
| Authors | Jiang, J.,Natarajan, K.,Kim, E.,Boyd, L.F.,Margulies, D.H. (deposition date: 2022-02-02, release date: 2022-09-07, Last modification date: 2024-10-23) |
| Primary citation | Jiang, J.,Taylor, D.K.,Kim, E.J.,Boyd, L.F.,Ahmad, J.,Mage, M.G.,Truong, H.V.,Woodward, C.H.,Sgourakis, N.G.,Cresswell, P.,Margulies, D.H.,Natarajan, K. Structural mechanism of tapasin-mediated MHC-I peptide loading in antigen presentation. Nat Commun, 13:5470-5470, 2022 Cited by PubMed 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 β-microglobulin interaction, leading to release of peptide. Movements of the membrane proximal Ig-like domains of tapasin, HLA-B*44:05, and β-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. PubMed: 36115831DOI: 10.1038/s41467-022-33153-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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