1rgo

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'''Structural Basis for Recognition of the mRNA Class II AU-Rich Element by the Tandem Zinc Finger Domain of TIS11d'''<br />
'''Structural Basis for Recognition of the mRNA Class II AU-Rich Element by the Tandem Zinc Finger Domain of TIS11d'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1RGO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RGO OCA].
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1RGO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RGO OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Dyson, H.J.]]
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[[Category: Dyson, H J.]]
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[[Category: Hudson, B.P.]]
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[[Category: Hudson, B P.]]
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[[Category: Martinez-Yamout, M.A.]]
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[[Category: Martinez-Yamout, M A.]]
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[[Category: Wright, P.E.]]
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[[Category: Wright, P E.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: tis11 ttp tristetraprolin butyrate response factor erf nup475 zfp zn zinc finger rna ss single-stranded are utr tandem intercalation intercalate specific]]
[[Category: tis11 ttp tristetraprolin butyrate response factor erf nup475 zfp zn zinc finger rna ss single-stranded are utr tandem intercalation intercalate specific]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:03:19 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:50:44 2008''

Revision as of 12:50, 21 February 2008


1rgo

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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 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

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