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4JXT

CID of human RPRD1A in complex with a phosphorylated peptide from RPB1-CTD

Summary for 4JXT
Entry DOI10.2210/pdb4jxt/pdb
DescriptorRegulation of nuclear pre-mRNA domain-containing protein 1A, DNA-directed RNA polymerase II subunit RPB1, UNKNOWN ATOM OR ION, ... (4 entities in total)
Functional Keywordsstructural genomics consortium, structural genomics, sgc, protein binding
Biological sourceHomo sapiens (human)
More
Cellular locationNucleus : P24928
Total number of polymer chains2
Total formula weight18506.68
Authors
Primary citationNi, Z.,Xu, C.,Guo, X.,Hunter, G.O.,Kuznetsova, O.V.,Tempel, W.,Marcon, E.,Zhong, G.,Guo, H.,Kuo, W.H.,Li, J.,Young, P.,Olsen, J.B.,Wan, C.,Loppnau, P.,El Bakkouri, M.,Senisterra, G.A.,He, H.,Huang, H.,Sidhu, S.S.,Emili, A.,Murphy, S.,Mosley, A.L.,Arrowsmith, C.H.,Min, J.,Greenblatt, J.F.
RPRD1A and RPRD1B are human RNA polymerase II C-terminal domain scaffolds for Ser5 dephosphorylation.
Nat.Struct.Mol.Biol., 21:686-695, 2014
Cited by
PubMed Abstract: The RNA polymerase II (RNAPII) C-terminal domain (CTD) heptapeptide repeats (1-YSPTSPS-7) undergo dynamic phosphorylation and dephosphorylation during the transcription cycle to recruit factors that regulate transcription, RNA processing and chromatin modification. We show here that RPRD1A and RPRD1B form homodimers and heterodimers through their coiled-coil domains and interact preferentially via CTD-interaction domains (CIDs) with RNAPII CTD repeats phosphorylated at S2 and S7. Crystal structures of the RPRD1A, RPRD1B and RPRD2 CIDs, alone and in complex with RNAPII CTD phosphoisoforms, elucidate the molecular basis of CTD recognition. In an example of cross-talk between different CTD modifications, our data also indicate that RPRD1A and RPRD1B associate directly with RPAP2 phosphatase and, by interacting with CTD repeats where phospho-S2 and/or phospho-S7 bracket a phospho-S5 residue, serve as CTD scaffolds to coordinate the dephosphorylation of phospho-S5 by RPAP2.
PubMed: 24997600
DOI: 10.1038/nsmb.2853
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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