5l85 | pdb_00005l85

Solution structure of the complex between human ZNHIT3 and NUFIP1 proteins

spinqualitylabelsall models 5l85 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5l85 is a 2 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ZNHI3_HUMAN Publication Abstract from PubMed Box C/D small nucleolar ribonucleoparticles (snoRNPs) support 2'-O-methylation of several target RNAs. They share a common set of four core proteins (SNU13, NOP58, NOP56, and FBL) that are assembled on different guide small nucleolar RNAs. Assembly of these entities involves additional protein factors that are absent in the mature active particle. In this context, the platform protein NUFIP1/Rsa1 establishes direct and simultaneous contacts with core proteins and with the components of the assembly machinery. Here, we solve the nuclear magnetic resonance (NMR) structure of a complex resulting from interaction between protein fragments of human NUFIP1 and its cofactor ZNHIT3, and emphasize their imbrication. Using yeast two-hybrid and complementation assays, protein co-expression, isothermal titration calorimetry, and NMR, we demonstrate that yeast and human complexes involving NUFIP1/Rsa1p, ZNHIT3/Hit1p, and SNU13/Snu13p share strong structural similarities, suggesting that the initial steps of the box C/D snoRNP assembly process are conserved among species. Structural Features of the Box C/D snoRNP Pre-assembly Process Are Conserved through Species.,Quinternet M, Chagot ME, Rothe B, Tiotiu D, Charpentier B, Manival X Structure. 2016 Sep 1. pii: S0969-2126(16)30227-1. doi:, 10.1016/j.str.2016.07.016. PMID:27594683 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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