2jpd

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(New page: 200px<br /> <applet load="2jpd" size="450" color="white" frame="true" align="right" spinBox="true" caption="2jpd" /> '''Solution structure of the ERCC1 central dom...)
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'''Solution structure of the ERCC1 central domain'''<br />
'''Solution structure of the ERCC1 central domain'''<br />
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==Overview==
==Overview==
Human ERCC1/XPF is a structure-specific endonuclease involved in multiple, DNA repair pathways. We present the solution structure of the, non-catalytic ERCC1 central domain. Although this domain shows structural, homology with the catalytically active XPF nuclease domain, functional, investigation reveals a completely distinct function for the ERCC1 central, domain by performing interactions with both XPA and single-stranded DNA., These interactions are non-competitive and can occur simultaneously, through distinct interaction surfaces. Interestingly, the XPA binding by, ERCC1 and the catalytic function of XPF are dependent on a structurally, homologous region of the two proteins. Although these regions are strictly, conserved in each protein family, amino acid composition and surface, characteristics are distinct. We discuss the possibility that after XPF, gene duplication, the redundant ERCC1 central domain acquired novel, functions, thereby increasing the fidelity of eukaryotic DNA repair.
Human ERCC1/XPF is a structure-specific endonuclease involved in multiple, DNA repair pathways. We present the solution structure of the, non-catalytic ERCC1 central domain. Although this domain shows structural, homology with the catalytically active XPF nuclease domain, functional, investigation reveals a completely distinct function for the ERCC1 central, domain by performing interactions with both XPA and single-stranded DNA., These interactions are non-competitive and can occur simultaneously, through distinct interaction surfaces. Interestingly, the XPA binding by, ERCC1 and the catalytic function of XPF are dependent on a structurally, homologous region of the two proteins. Although these regions are strictly, conserved in each protein family, amino acid composition and surface, characteristics are distinct. We discuss the possibility that after XPF, gene duplication, the redundant ERCC1 central domain acquired novel, functions, thereby increasing the fidelity of eukaryotic DNA repair.
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==Disease==
 
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Known disease associated with this structure: Cerebrooculofacioskeletal syndrome 4 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=126380 126380]]
 
==About this Structure==
==About this Structure==
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2JPD 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=2JPD OCA].
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2JPD 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=2JPD OCA].
==Reference==
==Reference==
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[[Category: protein]]
[[Category: protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:57:16 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:56:04 2008''

Revision as of 10:56, 23 January 2008


2jpd

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Solution structure of the ERCC1 central domain

Overview

Human ERCC1/XPF is a structure-specific endonuclease involved in multiple, DNA repair pathways. We present the solution structure of the, non-catalytic ERCC1 central domain. Although this domain shows structural, homology with the catalytically active XPF nuclease domain, functional, investigation reveals a completely distinct function for the ERCC1 central, domain by performing interactions with both XPA and single-stranded DNA., These interactions are non-competitive and can occur simultaneously, through distinct interaction surfaces. Interestingly, the XPA binding by, ERCC1 and the catalytic function of XPF are dependent on a structurally, homologous region of the two proteins. Although these regions are strictly, conserved in each protein family, amino acid composition and surface, characteristics are distinct. We discuss the possibility that after XPF, gene duplication, the redundant ERCC1 central domain acquired novel, functions, thereby increasing the fidelity of eukaryotic DNA repair.

About this Structure

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

Reference

Analysis of the XPA and ssDNA-binding surfaces on the central domain of human ERCC1 reveals evidence for subfunctionalization., Tripsianes K, Folkers GE, Zheng C, Das D, Grinstead JS, Kaptein R, Boelens R, Nucleic Acids Res. 2007 Aug 24;. PMID:17720715

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