1l3e

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[[Image:1l3e.gif|left|200px]]
[[Image:1l3e.gif|left|200px]]
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{{Structure
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|PDB= 1l3e |SIZE=350|CAPTION= <scene name='initialview01'>1l3e</scene>
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The line below this paragraph, containing "STRUCTURE_1l3e", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=Zn1:Zn+Coordinate+Site+1'>Zn1</scene>, <scene name='pdbsite=Zn2:Zn+Coordinate+Site+2'>Zn2</scene> and <scene name='pdbsite=Zn3:Zn+Coordinate+Site+3'>Zn3</scene>
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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|ACTIVITY=
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|GENE= hypoxia inducible factor-1 alpha ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), p300 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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{{STRUCTURE_1l3e| PDB=1l3e | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l3e OCA], [http://www.ebi.ac.uk/pdbsum/1l3e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1l3e RCSB]</span>
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'''NMR Structures of the HIF-1alpha CTAD/p300 CH1 Complex'''
'''NMR Structures of the HIF-1alpha CTAD/p300 CH1 Complex'''
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[[Category: Sun, Z J.]]
[[Category: Sun, Z J.]]
[[Category: Wagner, G.]]
[[Category: Wagner, G.]]
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[[Category: protein-protein complex]]
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[[Category: Protein-protein complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:29:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:57:27 2008''
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Revision as of 20:29, 2 May 2008

Image:1l3e.gif

Template:STRUCTURE 1l3e

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. 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 Fri May 2 23:29:40 2008

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