1l3e

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(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 ...)
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==About this Structure==
==About this Structure==
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1L3E is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with ZN as [[http://en.wikipedia.org/wiki/ligand ligand]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1L3E OCA]].
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1L3E is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with ZN as [[http://en.wikipedia.org/wiki/ligand ligand]]. Structure known Active Sites: Zn1, Zn2 and Zn3. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1L3E OCA]].
==Reference==
==Reference==
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[[Category: protein-protein complex]]
[[Category: protein-protein complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 17:19:24 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:05:59 2007''

Revision as of 09:01, 30 October 2007


1l3e

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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]. Structure known Active Sites: Zn1, Zn2 and Zn3. 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

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