1pfj

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="1pfj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pfj" /> '''Solution structure of the N-terminal PH/PTB...)
Line 1: Line 1:
-
[[Image:1pfj.gif|left|200px]]<br />
+
[[Image:1pfj.gif|left|200px]]<br /><applet load="1pfj" size="350" color="white" frame="true" align="right" spinBox="true"
-
<applet load="1pfj" size="450" color="white" frame="true" align="right" spinBox="true"
+
caption="1pfj" />
caption="1pfj" />
'''Solution structure of the N-terminal PH/PTB domain of the TFIIH P62 subunit'''<br />
'''Solution structure of the N-terminal PH/PTB domain of the TFIIH P62 subunit'''<br />
==Overview==
==Overview==
-
The human general transcription factor TFIIH is involved in both, transcription and DNA repair. We have identified a structural domain in, the core subunit of TFIIH, p62, which is absolutely required for DNA, repair activity through the nucleotide excision repair pathway. Using, coimmunoprecipitation experiments, we showed that this activity involves, the interaction between the N-terminal domain of p62 and the 3', endonuclease XPG, a major component of the nucleotide excision repair, machinery. Furthermore, we reconstituted a functional TFIIH particle with, a mutant of p62 lacking the N-terminal domain, showing that this domain is, not required for assembly of the TFIIH complex and basal transcription. We, solved its three-dimensional structure and found an unpredicted pleckstrin, homology and phosphotyrosine binding (PH/PTB) domain, uncovering a new, class of activity for this fold.
+
The human general transcription factor TFIIH is involved in both transcription and DNA repair. We have identified a structural domain in the core subunit of TFIIH, p62, which is absolutely required for DNA repair activity through the nucleotide excision repair pathway. Using coimmunoprecipitation experiments, we showed that this activity involves the interaction between the N-terminal domain of p62 and the 3' endonuclease XPG, a major component of the nucleotide excision repair machinery. Furthermore, we reconstituted a functional TFIIH particle with a mutant of p62 lacking the N-terminal domain, showing that this domain is not required for assembly of the TFIIH complex and basal transcription. We solved its three-dimensional structure and found an unpredicted pleckstrin homology and phosphotyrosine binding (PH/PTB) domain, uncovering a new class of activity for this fold.
==About this Structure==
==About this Structure==
-
1PFJ 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=1PFJ OCA].
+
1PFJ 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=1PFJ OCA].
==Reference==
==Reference==
Line 20: Line 19:
[[Category: Lamour, V.]]
[[Category: Lamour, V.]]
[[Category: Poterszman, A.]]
[[Category: Poterszman, A.]]
-
[[Category: SPINE, Structural.Proteomics.in.Europe.]]
+
[[Category: SPINE, Structural Proteomics in Europe.]]
-
[[Category: Thierry, J.C.]]
+
[[Category: Thierry, J C.]]
[[Category: Wasielewski, E.]]
[[Category: Wasielewski, E.]]
[[Category: ph/ptb domain]]
[[Category: ph/ptb domain]]
Line 28: Line 27:
[[Category: structural proteomics in europe]]
[[Category: structural proteomics in europe]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:42:59 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:28:13 2008''

Revision as of 12:28, 21 February 2008


1pfj

Drag the structure with the mouse to rotate

Solution structure of the N-terminal PH/PTB domain of the TFIIH P62 subunit

Overview

The human general transcription factor TFIIH is involved in both transcription and DNA repair. We have identified a structural domain in the core subunit of TFIIH, p62, which is absolutely required for DNA repair activity through the nucleotide excision repair pathway. Using coimmunoprecipitation experiments, we showed that this activity involves the interaction between the N-terminal domain of p62 and the 3' endonuclease XPG, a major component of the nucleotide excision repair machinery. Furthermore, we reconstituted a functional TFIIH particle with a mutant of p62 lacking the N-terminal domain, showing that this domain is not required for assembly of the TFIIH complex and basal transcription. We solved its three-dimensional structure and found an unpredicted pleckstrin homology and phosphotyrosine binding (PH/PTB) domain, uncovering a new class of activity for this fold.

About this Structure

1PFJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

TFIIH contains a PH domain involved in DNA nucleotide excision repair., Gervais V, Lamour V, Jawhari A, Frindel F, Wasielewski E, Dubaele S, Egly JM, Thierry JC, Kieffer B, Poterszman A, Nat Struct Mol Biol. 2004 Jul;11(7):616-22. Epub 2004 Jun 13. PMID:15195146

Page seeded by OCA on Thu Feb 21 14:28:13 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools