1j2x
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Crystal structure of RAP74 C-terminal domain complexed with FCP1 C-terminal peptide
OverviewOverview
After mRNA transcription termination in eukaryotes, the, hyperphosphorylated form of RNA polymerase II (pol II0) must be recycled, by TFIIF-associating C-terminal domain phosphatase (FCP1), the phosphatase, responsible for dephosphorylating the C-terminal domain of the largest, polymerase subunit. Transcription factor (TF)-IIF stimulates the activity, of FCP1, and the RNA polymerase II-associating protein 74 subunit of TFIIF, forms a complex with FCP1 in both human and yeast. Here, we report a, cocrystal structure of the winged-helix domain of human RNA polymerase, II-associating protein 74 bound to the alpha-helical C terminus of human, FCP1 (residues 944-961). These results illustrate the molecular mechanism, by which TFIIF efficiently recruits FCP1 to the pol II transcription, machinery for recycling of the polymerase.
DiseaseDisease
Known disease associated with this structure: Congenital cataracts, facial dysmorphism, and neuropathy OMIM:[604927]
About this StructureAbout this Structure
1J2X is a Protein complex structure of sequences from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Molecular mechanism of recruitment of TFIIF- associating RNA polymerase C-terminal domain phosphatase (FCP1) by transcription factor IIF., Kamada K, Roeder RG, Burley SK, Proc Natl Acad Sci U S A. 2003 Mar 4;100(5):2296-9. Epub 2003 Feb 18. PMID:12591941
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