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1RGO

Structural Basis for Recognition of the mRNA Class II AU-Rich Element by the Tandem Zinc Finger Domain of TIS11d

Summary for 1RGO
Entry DOI10.2210/pdb1rgo/pdb
NMR InformationBMRB: 6005
DescriptorRNA (5'-R(*UP*UP*AP*UP*UP*UP*AP*UP*U)-3'), Butyrate response factor 2, ZINC ION (3 entities in total)
Functional Keywordstis11 ttp tristetraprolin butyrate response factor erf nup475 zfp zn zinc finger rna ss single-stranded are utr tandem intercalation intercalate specific, rna binding protein
Biological sourceHomo sapiens (human)
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Cellular locationNucleus (Potential): P47974
Total number of polymer chains2
Total formula weight11202.88
Authors
Hudson, B.P.,Martinez-Yamout, M.A.,Dyson, H.J.,Wright, P.E. (deposition date: 2003-11-12, release date: 2004-03-02, Last modification date: 2024-05-22)
Primary citationHudson, B.P.,Martinez-Yamout, M.A.,Dyson, H.J.,Wright, P.E.
Recognition of the mRNA AU-rich element by the zinc finger domain of TIS11d.
NAT.STRUCT.MOL.BIOL., 11:257-264, 2004
Cited by
PubMed Abstract: The tandem zinc finger (TZF) domain of the protein TIS11d binds to the class II AU-rich element (ARE) in the 3' untranslated region (3' UTR) of target mRNAs and promotes their deadenylation and degradation. The NMR structure of the TIS11d TZF domain bound to the RNA sequence 5'-UUAUUUAUU-3' comprises a pair of novel CCCH fingers of type CX(8)CX(5)CX(3)H separated by an 18-residue linker. The two TIS11d zinc fingers bind in a symmetrical fashion to adjacent 5'-UAUU-3' subsites on the single-stranded RNA via a combination of electrostatic and hydrogen-bonding interactions, with intercalative stacking between conserved aromatic side chains and the RNA bases. Sequence specificity in RNA recognition is achieved by a network of intermolecular hydrogen bonds, mostly between TIS11d main-chain functional groups and the Watson-Crick edges of the bases. The TIS11d structure provides insights into the RNA-binding functions of this large family of CCCH zinc finger proteins.
PubMed: 14981510
DOI: 10.1038/nsmb738
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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