1xmk

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[[Image:1xmk.gif|left|200px]]
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{{STRUCTURE_1xmk| PDB=1xmk | SCENE= }}
{{STRUCTURE_1xmk| PDB=1xmk | SCENE= }}
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'''The Crystal structure of the Zb domain from the RNA editing enzyme ADAR1'''
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===The Crystal structure of the Zb domain from the RNA editing enzyme ADAR1===
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==Overview==
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The Zalpha domains represent a growing subfamily of the winged helix-turn-helix (HTH) domain family whose members share a remarkable ability to bind specifically to Z-DNA and/or Z-RNA. They have been found exclusively in proteins involved in interferon response and, while their importance in determining pox viral pathogenicity has been demonstrated, their actual target and biological role remain obscure. Cellular proteins containing Zalpha domains bear a second homologous domain termed Zbeta, which appears to lack the ability to bind left-handed nucleic acids. Here, we present the crystal structure of the Zbeta domain from the human double-stranded RNA adenosine deaminase ADAR1 at 0.97 A, determined by single isomorphous replacement including anomalous scattering. Zbeta maintains a winged-HTH fold with the addition of a C-terminal helix. Mapping of the Zbeta conservation profile on the Zbeta surface reveals a new conserved surface formed partly by the terminal helix 4, involved in metal binding and dimerization and absent from Zalpha domains. Our results show how two domains similar in fold may have evolved into different functional entities even in the context of the same protein.
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The line below this paragraph, {{ABSTRACT_PUBMED_16023667}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 16023667 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16023667}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
The crystal structure of the Zbeta domain of the RNA-editing enzyme ADAR1 reveals distinct conserved surfaces among Z-domains., Athanasiadis A, Placido D, Maas S, Brown BA 2nd, Lowenhaupt K, Rich A, J Mol Biol. 2005 Aug 19;351(3):496-507. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16023667 16023667]
The crystal structure of the Zbeta domain of the RNA-editing enzyme ADAR1 reveals distinct conserved surfaces among Z-domains., Athanasiadis A, Placido D, Maas S, Brown BA 2nd, Lowenhaupt K, Rich A, J Mol Biol. 2005 Aug 19;351(3):496-507. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16023667 16023667]
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Structure of the DLM-1-Z-DNA complex reveals a conserved family of Z-DNA-binding proteins., Schwartz T, Behlke J, Lowenhaupt K, Heinemann U, Rich A, Nat Struct Biol. 2001 Sep;8(9):761-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11524677 11524677]
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Crystal structure of the Zalpha domain of the human editing enzyme ADAR1 bound to left-handed Z-DNA., Schwartz T, Rould MA, Lowenhaupt K, Herbert A, Rich A, Science. 1999 Jun 11;284(5421):1841-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10364558 10364558]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Rna editing]]
[[Category: Rna editing]]
[[Category: Winged helix-turn-helix]]
[[Category: Winged helix-turn-helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:13:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:55:03 2008''

Revision as of 00:55, 29 July 2008

Template:STRUCTURE 1xmk

The Crystal structure of the Zb domain from the RNA editing enzyme ADAR1

Template:ABSTRACT PUBMED 16023667

About this Structure

1XMK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The crystal structure of the Zbeta domain of the RNA-editing enzyme ADAR1 reveals distinct conserved surfaces among Z-domains., Athanasiadis A, Placido D, Maas S, Brown BA 2nd, Lowenhaupt K, Rich A, J Mol Biol. 2005 Aug 19;351(3):496-507. PMID:16023667

Structure of the DLM-1-Z-DNA complex reveals a conserved family of Z-DNA-binding proteins., Schwartz T, Behlke J, Lowenhaupt K, Heinemann U, Rich A, Nat Struct Biol. 2001 Sep;8(9):761-5. PMID:11524677

Crystal structure of the Zalpha domain of the human editing enzyme ADAR1 bound to left-handed Z-DNA., Schwartz T, Rould MA, Lowenhaupt K, Herbert A, Rich A, Science. 1999 Jun 11;284(5421):1841-5. PMID:10364558

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