2axl

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2axl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2axl OCA], [http://www.ebi.ac.uk/pdbsum/2axl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2axl RCSB]</span>
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'''Solution structure of a multifunctional DNA- and protein-binding domain of human Werner syndrome protein'''
'''Solution structure of a multifunctional DNA- and protein-binding domain of human Werner syndrome protein'''
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[[Category: Xi, X G.]]
[[Category: Xi, X G.]]
[[Category: Zeng, W.]]
[[Category: Zeng, W.]]
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[[Category: the wh-like domain]]
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[[Category: The wh-like domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:35:52 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:58:41 2008''
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Revision as of 16:35, 3 May 2008

Template:STRUCTURE 2axl

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


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.

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 Page seeded by OCA on Sat May 3 19:35:52 2008

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