2axl

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(New page: 200px<br /> <applet load="2axl" size="450" color="white" frame="true" align="right" spinBox="true" caption="2axl" /> '''Solution structure of a multifunctional DNA...)
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'''Solution structure of a multifunctional DNA- and protein-binding domain of human Werner syndrome protein'''<br />
'''Solution structure of a multifunctional DNA- and protein-binding domain of human Werner syndrome protein'''<br />
==Overview==
==Overview==
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Werner syndrome (WS) is an autosomal recessive disease that results in, premature aging. Mutations in the WS gene (WRN) result in a loss of, expression of the WRN protein and predispose WS patients to accelerated, aging. As a helicase and a nuclease, WRN is unique among the five human, RecQ helicase family members and is capable of multiple functions involved, in DNA replication, repair, recombination, and telomere maintenance. A, 144-residue fragment of WRN was previously determined to be a, multifunctional DNA- and protein-binding domain (DPBD) that interacts with, structure-specific DNA and a variety of DNA-processing proteins. In, addition, DPBD functions as a nucleolar targeting sequence of WRN. The, solution structure of the DPBD, the first of a WRN fragment, has been, solved by NMR. DPBD consists of a winged helix-like motif and an, unstructured C-terminal region of approximately 20 aa. The putative, DNA-binding surface of DPBD has been identified by using known structural, and biochemical data. Based on the structural data and on the biochemical, data, we suggest a surface on the DPBD for interacting with other, proteins. In this structural model, a single winged helix domain binds to, both DNA and other proteins. Furthermore, we propose that DPBD functions, as a regulatory domain to regulate the enzymatic activity of WRN and to, direct cellular localization of WRN through protein-protein interaction.
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Werner syndrome (WS) is an autosomal recessive disease that results in premature aging. Mutations in the WS gene (WRN) result in a loss of expression of the WRN protein and predispose WS patients to accelerated aging. As a helicase and a nuclease, WRN is unique among the five human RecQ helicase family members and is capable of multiple functions involved in DNA replication, repair, recombination, and telomere maintenance. A 144-residue fragment of WRN was previously determined to be a multifunctional DNA- and protein-binding domain (DPBD) that interacts with structure-specific DNA and a variety of DNA-processing proteins. In addition, DPBD functions as a nucleolar targeting sequence of WRN. The solution structure of the DPBD, the first of a WRN fragment, has been solved by NMR. DPBD consists of a winged helix-like motif and an unstructured C-terminal region of approximately 20 aa. The putative DNA-binding surface of DPBD has been identified by using known structural and biochemical data. Based on the structural data and on the biochemical data, we suggest a surface on the DPBD for interacting with other proteins. In this structural model, a single winged helix domain binds to both DNA and other proteins. Furthermore, we propose that DPBD functions as a regulatory domain to regulate the enzymatic activity of WRN and to direct cellular localization of WRN through protein-protein interaction.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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2AXL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2AXL OCA].
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2AXL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AXL OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Feng, H.]]
[[Category: Feng, H.]]
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[[Category: Hu, J.S.]]
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[[Category: Hu, J S.]]
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[[Category: Lin, G.X.]]
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[[Category: Lin, G X.]]
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[[Category: Xi, X.G.]]
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[[Category: Xi, X G.]]
[[Category: Zeng, W.]]
[[Category: Zeng, W.]]
[[Category: the wh-like domain]]
[[Category: the wh-like domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:55:59 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:32:02 2008''

Revision as of 14:32, 21 February 2008


2axl

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Solution structure of a multifunctional DNA- and protein-binding domain of human Werner syndrome protein

Contents

Overview

Werner syndrome (WS) is an autosomal recessive disease that results in premature aging. Mutations in the WS gene (WRN) result in a loss of expression of the WRN protein and predispose WS patients to accelerated aging. As a helicase and a nuclease, WRN is unique among the five human RecQ helicase family members and is capable of multiple functions involved in DNA replication, repair, recombination, and telomere maintenance. A 144-residue fragment of WRN was previously determined to be a multifunctional DNA- and protein-binding domain (DPBD) that interacts with structure-specific DNA and a variety of DNA-processing proteins. In addition, DPBD functions as a nucleolar targeting sequence of WRN. The solution structure of the DPBD, the first of a WRN fragment, has been solved by NMR. DPBD consists of a winged helix-like motif and an unstructured C-terminal region of approximately 20 aa. The putative DNA-binding surface of DPBD has been identified by using known structural and biochemical data. Based on the structural data and on the biochemical data, we suggest a surface on the DPBD for interacting with other proteins. In this structural model, a single winged helix domain binds to both DNA and other proteins. Furthermore, we propose that DPBD functions as a regulatory domain to regulate the enzymatic activity of WRN and to direct cellular localization of WRN through protein-protein interaction.

Disease

Known diseases associated with this structure: Werner syndrome OMIM:[604611]

About this Structure

2AXL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Solution structure of a multifunctional DNA- and protein-binding motif of human Werner syndrome protein., Hu JS, Feng H, Zeng W, Lin GX, Xi XG, Proc Natl Acad Sci U S A. 2005 Dec 20;102(51):18379-84. Epub 2005 Dec 9. PMID:16339893

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