1rgo
From Proteopedia
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Structural Basis for Recognition of the mRNA Class II AU-Rich Element by the Tandem Zinc Finger Domain of TIS11d
Overview
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.
About this Structure
1RGO is a Single protein structure of sequence from Homo sapiens with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Recognition of the mRNA AU-rich element by the zinc finger domain of TIS11d., Hudson BP, Martinez-Yamout MA, Dyson HJ, Wright PE, Nat Struct Mol Biol. 2004 Mar;11(3):257-64. Epub 2004 Feb 8. PMID:14981510
Page seeded by OCA on Mon Nov 12 19:03:19 2007
