2gxb

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==Overview==
==Overview==
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The A form RNA double helix can be transformed to a left-handed helix, called Z-RNA. Currently, little is known about the detailed structural, features of Z-RNA or its involvement in cellular processes. The discovery, that certain interferon-response proteins have domains that can stabilize, Z-RNA as well as Z-DNA opens the way for the study of Z-RNA. Here, we, present the 2.25 A crystal structure of the Zalpha domain of the, RNA-editing enzyme ADAR1 (double-stranded RNA adenosine deaminase), complexed to a dUr(CG)(3) duplex RNA. The Z-RNA helix is associated with a, unique solvent pattern that distinguishes it from the otherwise similar, conformation of Z-DNA. Based on the structure, we propose a model, suggesting how differences in solvation lead to two types of Z-RNA, structures. The interaction of Zalpha with Z-RNA demonstrates how the, interferon-induced isoform of ADAR1 could be targeted toward selected, dsRNAs containing purine-pyrimidine repeats, possibly of viral origin.
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The A form RNA double helix can be transformed to a left-handed helix, called Z-RNA. Currently, little is known about the detailed structural features of Z-RNA or its involvement in cellular processes. The discovery that certain interferon-response proteins have domains that can stabilize Z-RNA as well as Z-DNA opens the way for the study of Z-RNA. Here, we present the 2.25 A crystal structure of the Zalpha domain of the RNA-editing enzyme ADAR1 (double-stranded RNA adenosine deaminase) complexed to a dUr(CG)(3) duplex RNA. The Z-RNA helix is associated with a unique solvent pattern that distinguishes it from the otherwise similar conformation of Z-DNA. Based on the structure, we propose a model suggesting how differences in solvation lead to two types of Z-RNA structures. The interaction of Zalpha with Z-RNA demonstrates how the interferon-induced isoform of ADAR1 could be targeted toward selected dsRNAs containing purine-pyrimidine repeats, possibly of viral origin.
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==Disease==
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Known diseases associated with this structure: Dyschromatosis symmetrica hereditaria OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=601059 601059]]
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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A Left-Handed RNA Double Helix Bound by the Zalpha Domain of the RNA-Editing Enzyme ADAR1., Placido D, Brown BA 2nd, Lowenhaupt K, Rich A, Athanasiadis A, Structure. 2007 Apr;15(4):395-404. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17437712 17437712]
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A left-handed RNA double helix bound by the Z alpha domain of the RNA-editing enzyme ADAR1., Placido D, Brown BA 2nd, Lowenhaupt K, Rich A, Athanasiadis A, Structure. 2007 Apr;15(4):395-404. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17437712 17437712]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: za]]
[[Category: za]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:26:52 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:36:16 2008''

Revision as of 15:36, 21 February 2008


2gxb, resolution 2.25Å

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Crystal Structure of The Za Domain bound to Z-RNA

Contents

Overview

The A form RNA double helix can be transformed to a left-handed helix, called Z-RNA. Currently, little is known about the detailed structural features of Z-RNA or its involvement in cellular processes. The discovery that certain interferon-response proteins have domains that can stabilize Z-RNA as well as Z-DNA opens the way for the study of Z-RNA. Here, we present the 2.25 A crystal structure of the Zalpha domain of the RNA-editing enzyme ADAR1 (double-stranded RNA adenosine deaminase) complexed to a dUr(CG)(3) duplex RNA. The Z-RNA helix is associated with a unique solvent pattern that distinguishes it from the otherwise similar conformation of Z-DNA. Based on the structure, we propose a model suggesting how differences in solvation lead to two types of Z-RNA structures. The interaction of Zalpha with Z-RNA demonstrates how the interferon-induced isoform of ADAR1 could be targeted toward selected dsRNAs containing purine-pyrimidine repeats, possibly of viral origin.

Disease

Known diseases associated with this structure: Dyschromatosis symmetrica hereditaria OMIM:[601059]

About this Structure

2GXB is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

A left-handed RNA double helix bound by the Z alpha domain of the RNA-editing enzyme ADAR1., Placido D, Brown BA 2nd, Lowenhaupt K, Rich A, Athanasiadis A, Structure. 2007 Apr;15(4):395-404. PMID:17437712

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