RPRD1A and RPRD1B are human RNA polymerase II C-terminal domain scaffolds for Ser5 dephosphorylation

Nature Structural and Molecular Biology

Volumn 21, Issue 8, 2014, Pages 686-695

  Ni, Zuyao ^a   Xu, Chao ^b   Guo, Xinghua ^a   Hunter, Gerald O ^c   Kuznetsova, Olga V ^d   Tempel, Wolfram ^b   Marcon, Edyta ^a   Zhong, Guoqing ^a   Guo, Hongbo ^a   Kuo, Wei Hung William ^a   Li, Joyce ^a   Young, Peter ^a   Olsen, Jonathan B ^a   Wan, Cuihong ^a   Loppnau, Peter ^b   El Bakkouri, Majida ^b   Senisterra, Guillermo A ^b   He, Hao ^b   Huang, Haiming ^a   Sidhu, Sachdev S ^a   Emili, Andrew ^a   Murphy, Shona ^d   Mosley, Amber L ^c   Arrowsmith, Cheryl H ^a,b   Min, Jinrong ^a,b   Greenblatt, Jack F ^a   more..

^a UNIVERSITY OF TORONTO   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

^c INDIANA UNIVERSITY SCHOOL OF MEDICINE   (United States)

^d UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

HEPTAPEPTIDE; HETERODIMER; HOMODIMER; PHOSPHATASE; PROTEIN RPAP2; PROTEIN RPRD1A; PROTEIN RPRD1B; PROTEIN RPRD2; RNA POLYMERASE II; SCAFFOLD PROTEIN; SERINE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CHROMATIN; COMPLEX FORMATION; CRYSTAL STRUCTURE; HUMAN; HUMAN CELL; MOLECULAR DYNAMICS; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEPHOSPHORYLATION; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; RNA PROCESSING; TRANSCRIPTION REGULATION;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CARRIER PROTEINS; CELL CYCLE PROTEINS; CRYSTALLOGRAPHY, X-RAY; HEK293 CELLS; HUMANS; HYDROGEN BONDING; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NEOPLASM PROTEINS; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN MULTIMERIZATION; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; REPRESSOR PROTEINS; RNA POLYMERASE II; SERINE;

EID: 84906101596     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2853     Document Type: Article

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