1fzj | pdb_00001fzj

MHC CLASS I NATURAL MUTANT H-2KBM1 HEAVY CHAIN COMPLEXED WITH BETA-2 MICROGLOBULIN AND VESICULAR STOMATITIS VIRUS NUCLEOPROTEIN

spinqualitylabelsall models 1fzj, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1fzj is a 3 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MPD, NAG, PO4, FUL NonStd Res: CSO Related: 1fzk, 1fzm, 1fzo, 2vaa, 2vab Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [HA1B_MOUSE] Involved in the presentation of foreign antigens to the immune system. [NCAP_VSIVG] Encapsidates the genome in a ratio of one N per nine ribonucleotides, protecting it from nucleases. The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication. Replication is dependent on intracellular concentration of newly synthesized N, termed N(0), which corresponds to the protein not associated with RNA. In contrast, when associated with RNA, it is termed N. During replication, encapsidation by N(0) is coupled to RNA synthesis and all replicative products are resistant to nucleases (By similarity). [B2MG_MOUSE] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The K(bm1) and K(bm8) natural mutants of the murine MHC class I molecule H-2K(b) were originally identified by allograft rejection. They also bind viral peptides VSV8 and SEV9 with high affinity, but their peptide complexes have substantially decreased thermostability, and the K(bm1) complexes do not elicit alloreactive T cell responses. Crystal structures of the four mutant complexes at 1.7-1.9 A resolution are similar to the corresponding wild-type K(b) structures, except in the vicinity of the mutated residues, which alter the electrostatic potential, topology, hydrogen bonding, and local water structure of the peptide binding groove. Thus, these natural K(b) mutations define the minimal perturbations in the peptide environment that alter antigen presentation to T cells and abolish alloreactivity. The crystal structures of K(bm1) and K(bm8) reveal that subtle changes in the peptide environment impact thermostability and alloreactivity.,Rudolph MG, Speir JA, Brunmark A, Mattsson N, Jackson MR, Peterson PA, Teyton L, Wilson IA Immunity. 2001 Mar;14(3):231-42. PMID:11290333 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-2 microglobulin 3D structures MHC 3D structures

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