2jpd
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Human ERCC1/XPF is a structure-specific endonuclease involved in multiple | + | 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== | ||
| + | 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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==Reference== | ==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 | + | 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;35(17):5789-98. Epub 2007 Aug 24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17720715 17720715] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Das, D.]] | [[Category: Das, D.]] | ||
[[Category: Folkers, G.]] | [[Category: Folkers, G.]] | ||
| - | [[Category: Grinstead, J | + | [[Category: Grinstead, J S.]] |
[[Category: Kaptein, R.]] | [[Category: Kaptein, R.]] | ||
[[Category: Tripsianes, K.]] | [[Category: Tripsianes, K.]] | ||
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[[Category: protein]] | [[Category: protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:04:52 2008'' |
Revision as of 16:04, 21 February 2008
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Solution structure of the ERCC1 central domain
Contents |
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.
Disease
Known disease associated with this structure: Cerebrooculofacioskeletal syndrome 4 OMIM:[126380]
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;35(17):5789-98. Epub 2007 Aug 24. PMID:17720715
Page seeded by OCA on Thu Feb 21 18:04:52 2008
