2jnj
From Proteopedia
(New page: 200px<br /> <applet load="2jnj" size="450" color="white" frame="true" align="right" spinBox="true" caption="2jnj" /> '''Solution structure of the p8 TFIIH subunit'...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2jnj.gif|left|200px]]<br /> | + | [[Image:2jnj.gif|left|200px]]<br /><applet load="2jnj" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2jnj" size=" | + | |
caption="2jnj" /> | caption="2jnj" /> | ||
'''Solution structure of the p8 TFIIH subunit'''<br /> | '''Solution structure of the p8 TFIIH subunit'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Trichothiodystrophy (TTD) is a rare hereditary multi-system disorder | + | Trichothiodystrophy (TTD) is a rare hereditary multi-system disorder associated with defects in nucleotide excision repair (NER) and transcription as consequences of mutations in XPB, XPD and p8/TTD-A subunits of transcription factor IIH (TFIIH). Here, we report the solution structure of the p8/TTD-A protein, a small alpha/beta protein built around an antiparallel beta-sheet that forms a homodimer with an extended interface. In order to characterize the dimer interface, we have introduced a mutation at position 44, which destabilizes the dimeric form of the protein. We have shown that this mutation has no effect on the intrinsic ability of p8/TTD-A to stimulate NER in vitro, but affects the capacity of p8/TTD-A to restore TFIIH concentration in TTD-A fibroblasts. Point mutations found in TTD-A patients are discussed on the basis of the present structure. |
==Disease== | ==Disease== | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2JNJ 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:// | + | 2JNJ 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=2JNJ OCA]. |
==Reference== | ==Reference== | ||
| - | Solution | + | Solution structure and self-association properties of the p8 TFIIH subunit responsible for trichothiodystrophy., Vitorino M, Coin F, Zlobinskaya O, Atkinson RA, Moras D, Egly JM, Poterszman A, Kieffer B, J Mol Biol. 2007 Apr 27;368(2):473-80. Epub 2007 Feb 20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17350038 17350038] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Atkinson, R | + | [[Category: Atkinson, R A.]] |
[[Category: Kieffer, B.]] | [[Category: Kieffer, B.]] | ||
[[Category: Moras, D.]] | [[Category: Moras, D.]] | ||
| Line 24: | Line 23: | ||
[[Category: protein]] | [[Category: protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:04:24 2008'' |
Revision as of 16:04, 21 February 2008
|
Solution structure of the p8 TFIIH subunit
Contents |
Overview
Trichothiodystrophy (TTD) is a rare hereditary multi-system disorder associated with defects in nucleotide excision repair (NER) and transcription as consequences of mutations in XPB, XPD and p8/TTD-A subunits of transcription factor IIH (TFIIH). Here, we report the solution structure of the p8/TTD-A protein, a small alpha/beta protein built around an antiparallel beta-sheet that forms a homodimer with an extended interface. In order to characterize the dimer interface, we have introduced a mutation at position 44, which destabilizes the dimeric form of the protein. We have shown that this mutation has no effect on the intrinsic ability of p8/TTD-A to stimulate NER in vitro, but affects the capacity of p8/TTD-A to restore TFIIH concentration in TTD-A fibroblasts. Point mutations found in TTD-A patients are discussed on the basis of the present structure.
Disease
Known disease associated with this structure: Trichothiodystrophy, complementation group A OMIM:[608780]
About this Structure
2JNJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure and self-association properties of the p8 TFIIH subunit responsible for trichothiodystrophy., Vitorino M, Coin F, Zlobinskaya O, Atkinson RA, Moras D, Egly JM, Poterszman A, Kieffer B, J Mol Biol. 2007 Apr 27;368(2):473-80. Epub 2007 Feb 20. PMID:17350038
Page seeded by OCA on Thu Feb 21 18:04:24 2008
