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.
1l3e
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1l3e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l3e" /> '''NMR Structures of the HIF-1alpha CTAD/p300 ...)
Next diff →
Revision as of 15:14, 29 October 2007
|
NMR Structures of the HIF-1alpha CTAD/p300 CH1 Complex
Overview
Adaptation to hypoxia is mediated by transactivation of hypoxia-responsive, genes by hypoxia-inducible factor-1 (HIF-1) in complex with the CBP and, p300 transcriptional coactivators. We report the solution structure of the, cysteine/histidine-rich 1 (CH1) domain of p300 bound to the C-terminal, transactivation domain of HIF-1 alpha. CH1 has a triangular geometry, composed of four alpha-helices with three intervening Zn(2+)-coordinating, centers. CH1 serves as a scaffold for folding of the HIF-1 alpha, C-terminal transactivation domain, which forms a vise-like clamp on the, CH1 domain that is stabilized by extensive hydrophobic and polar, interactions. The structure reveals the mechanism of specific recognition, of p300 by HIF-1 alpha, and shows how HIF-1 alpha transactivation is, ... [(full description)]
About this Structure
1L3E is a [Protein complex] structure of sequences from [Homo sapiens] with ZN as [ligand]. Full crystallographic information is available from [OCA].
Reference
Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1 alpha., Freedman SJ, Sun ZY, Poy F, Kung AL, Livingston DM, Wagner G, Eck MJ, Proc Natl Acad Sci U S A. 2002 Apr 16;99(8):5367-72. PMID:11959990
Page seeded by OCA on Mon Oct 29 17:19:24 2007
