5wer

Crystal Structure of TAPBPR and H2-Dd complex

spinqualitylabelsall models 5wer, resolution 3.41Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5wer is a 12 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.412Å Ligands: 1PE, CIT, EDO, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HA12_MOUSE Involved in the presentation of foreign antigens to the immune system. Publication Abstract from PubMed Central to CD8+ T-cell mediated immunity is the recognition of peptide-major histocompatibility complex class I (pMHC-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. Crystal structure of a TAPBPR-MHC-I complex reveals the mechanism of peptide editing in antigen presentation.,Jiang J, Natarajan K, Boyd LF, Morozov GI, Mage MG, Margulies DH Science. 2017 Oct 12. pii: eaao5154. doi: 10.1126/science.aao5154. PMID:29025991 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-2 microglobulin 3D structures

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