2e1f
From Proteopedia
(New page: 200px<br /> <applet load="2e1f" size="450" color="white" frame="true" align="right" spinBox="true" caption="2e1f, resolution 2.0Å" /> '''Crystal structure of...) |
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caption="2e1f, resolution 2.0Å" /> | caption="2e1f, resolution 2.0Å" /> | ||
'''Crystal structure of the HRDC Domain of Human Werner Syndrome Protein, WRN'''<br /> | '''Crystal structure of the HRDC Domain of Human Werner Syndrome Protein, WRN'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2E1F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2E1F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E1F OCA]. |
==Reference== | ==Reference== | ||
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[[Category: hrdc domain]] | [[Category: hrdc domain]] | ||
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Revision as of 15:23, 15 February 2008
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Crystal structure of the HRDC Domain of Human Werner Syndrome Protein, WRN
Contents |
Overview
Werner syndrome is a human premature aging disorder characterized by, chromosomal instability. The disease is caused by the functional loss of, WRN, a member of the RecQ-helicase family that plays an important role in, DNA metabolic pathways. WRN contains four structurally folded domains, comprising an exonuclease, a helicase, a winged-helix, and a, helicase-and-ribonuclease D/C-terminal (HRDC) domain. In contrast to the, accumulated knowledge pertaining to the biochemical functions of the three, N-terminal domains, the function of C-terminal HRDC remains unknown. In, this study, the crystal structure of the human WRN HRDC domain has been, determined. The domain forms a bundle of alpha-helices similar to those of, Saccharomyces cerevisiae Sgs1 and Escherichia coli RecQ. Surprisingly, the, extra ten residues at each of the N and C termini of the domain were found, to participate in the domain architecture by forming an extended portion, of the first helix alpha1, and a novel looping motif that traverses, straight along the domain surface, respectively. The motifs combine to, increase the domain surface of WRN HRDC, which is larger than that of Sgs1, and E. coli.In WRN HRDC, neither of the proposed DNA-binding surfaces in, Sgs1 or E. coli is conserved, and the domain was shown to lack DNA-binding, ability in vitro. Moreover, the domain was shown to be thermostable and, resistant to protease digestion, implying independent domain evolution in, WRN. Coupled with the unique long linker region in WRN, the WRN HRDC may, be adapted to play a distinct function in WRN that involves, protein-protein interactions.
Disease
Known diseases associated with this structure: Werner syndrome OMIM:[604611]
About this Structure
2E1F is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of the HRDC domain of human Werner syndrome protein, WRN., Kitano K, Yoshihara N, Hakoshima T, J Biol Chem. 2007 Jan 26;282(4):2717-28. Epub 2006 Dec 4. PMID:17148451
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