1l3e
From Proteopedia
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Revision as of 14:36, 5 November 2007
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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, regulated by asparagine hydroxylation.
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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