This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2rnr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2rnr.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2rnr.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2rnr| PDB=2rnr | SCENE= }}
{{STRUCTURE_2rnr| PDB=2rnr | SCENE= }}
-
'''Solution structure of the complex between TFIIE alpha C-terminal acidic domain and TFIIH p62 PH domain'''
+
===Solution structure of the complex between TFIIE alpha C-terminal acidic domain and TFIIH p62 PH domain===
-
==Overview==
+
<!--
-
RNA polymerase II and general transcription factors (GTFs) assemble on a promoter to form a transcription preinitiation complex (PIC). Among the GTFs, TFIIE recruits TFIIH to complete the PIC formation and regulates enzymatic activities of TFIIH. However, the mode of binding between TFIIE and TFIIH is poorly understood. Here, we demonstrate the specific binding of the C-terminal acidic domain (AC-D) of the human TFIIEalpha subunit to the pleckstrin homology domain (PH-D) of the human TFIIH p62 subunit and describe the solution structures of the free and PH-D-bound forms of AC-D. Although the flexible N-terminal acidic tail from AC-D wraps around PH-D, the core domain of AC-D also interacts with PH-D. AC-D employs an entirely novel binding mode, which differs from the amphipathic helix method used by many transcriptional activators. So the binding surface between PH-D and AC-D is much broader than the specific binding surface between PH-D and the p53 acidic fragments. From our in vitro studies, we demonstrate that this interaction could be a switch to replace p53 with TFIIE on TFIIH in transcription.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18354501}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18354501 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18354501}}
==About this Structure==
==About this Structure==
-
2RNR is a [[Protein complex]] structure of sequences 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=2RNR OCA].
+
2RNR is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RNR OCA].
==Reference==
==Reference==
Line 31: Line 35:
[[Category: Human tfiih p62]]
[[Category: Human tfiih p62]]
[[Category: Ph domain]]
[[Category: Ph domain]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 24 09:29:50 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:56:52 2008''

Revision as of 06:56, 28 July 2008

Image:2rnr.png

Template:STRUCTURE 2rnr

Solution structure of the complex between TFIIE alpha C-terminal acidic domain and TFIIH p62 PH domain

Template:ABSTRACT PUBMED 18354501

About this Structure

2RNR is a Protein complex structure of sequences from Homo sapiens. Full experimental information is available from OCA.

Reference

Structural insight into the TFIIE-TFIIH interaction: TFIIE and p53 share the binding region on TFIIH., Okuda M, Tanaka A, Satoh M, Mizuta S, Takazawa M, Ohkuma Y, Nishimura Y, EMBO J. 2008 Mar 20;. PMID:18354501

Page seeded by OCA on Mon Jul 28 09:56:52 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2rnr"
Personal tools