1l3e
From Proteopedia
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| - | [[Image:1l3e.gif|left|200px]]<br /><applet load="1l3e" size=" | + | [[Image:1l3e.gif|left|200px]]<br /><applet load="1l3e" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1l3e" /> | caption="1l3e" /> | ||
'''NMR Structures of the HIF-1alpha CTAD/p300 CH1 Complex'''<br /> | '''NMR Structures of the HIF-1alpha CTAD/p300 CH1 Complex'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 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]. Known structural/functional Sites: <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>. Full crystallographic information is available from [http:// | + | 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 <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <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>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L3E OCA]. |
==Reference== | ==Reference== | ||
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[[Category: protein-protein complex]] | [[Category: protein-protein complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:53:10 2008'' |
Revision as of 07:53, 3 February 2008
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NMR Structures of the HIF-1alpha CTAD/p300 CH1 Complex
Contents |
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.
Disease
Known diseases associated with this structure: Colorectal cancer OMIM:[602700], Rubinstein-Taybi syndrome OMIM:[602700]
About this Structure
1L3E is a Protein complex structure of sequences from Homo sapiens with as ligand. Known structural/functional Sites: , and . 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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