2lo6

Structure of Nrd1 CID bound to phosphorylated RNAP II CTD

spinqualitylabelsall models 2lo6 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2lo6 is a 2 chain structure with sequence from Saccharomyces cerevisiae S288C. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 20 models Ligands: SEP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NRD1_YEAST Plays a role in sequence-specific regulation of nuclear pre-mRNA abundance. Publication Abstract from PubMed Recruitment of appropriate RNA processing factors to the site of transcription is controlled by post-translational modifications of the C-terminal domain (CTD) of RNA polymerase II (RNAP II). Here, we report the solution structure of the Ser5 phosphorylated (pSer5) CTD bound to Nrd1. The structure reveals a direct recognition of pSer5 by Nrd1 that requires the cis conformation of the upstream pSer5-Pro6 peptidyl-prolyl bond of the CTD. Mutations at the complex interface diminish binding affinity and impair processing or degradation of noncoding RNAs. These findings underpin the interplay between covalent and noncovalent changes in the CTD structure that constitute the CTD code. Serine phosphorylation and proline isomerization in RNAP II CTD control recruitment of Nrd1.,Kubicek K, Cerna H, Holub P, Pasulka J, Hrossova D, Loehr F, Hofr C, Vanacova S, Stefl R Genes Dev. 2012 Sep 1;26(17):1891-6. doi: 10.1101/gad.192781.112. Epub 2012 Aug, 14. PMID:22892239 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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