7tud

Crystal structure of HLA-B*44:05 (T73C) with 6mer EEFGRC and dipeptide GL

spinqualitylabelsall models 7tud, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7tud is a 4 chain structure with sequence from Homo sapiens and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.45Å Ligands: EDO, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D5H3J5_HUMAN Publication Abstract from PubMed 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 beta(2)-microglobulin interaction, leading to release of peptide. Movements of the membrane proximal Ig-like domains of tapasin, HLA-B*44:05, and beta(2)-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. Structural mechanism of tapasin-mediated MHC-I peptide loading in antigen presentation.,Jiang J, Taylor DK, Kim EJ, Boyd LF, Ahmad J, Mage MG, Truong HV, Woodward CH, Sgourakis NG, Cresswell P, Margulies DH, Natarajan K Nat Commun. 2022 Sep 17;13(1):5470. doi: 10.1038/s41467-022-33153-8. PMID:36115831 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-2 microglobulin 3D structures

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