2qc9

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[[Image:2qc9.jpg|left|200px]]
[[Image:2qc9.jpg|left|200px]]
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{{Structure
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|PDB= 2qc9 |SIZE=350|CAPTION= <scene name='initialview01'>2qc9</scene>, resolution 2.350&Aring;
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The line below this paragraph, containing "STRUCTURE_2qc9", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=AHB:BETA-HYDROXYASPARAGINE'>AHB</scene>
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|GENE= Notch1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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|DOMAIN=
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{{STRUCTURE_2qc9| PDB=2qc9 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qc9 OCA], [http://www.ebi.ac.uk/pdbsum/2qc9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qc9 RCSB]</span>
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'''Mouse Notch 1 Ankyrin Repeat Intracellular Domain'''
'''Mouse Notch 1 Ankyrin Repeat Intracellular Domain'''
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[[Category: McDonough, M A.]]
[[Category: McDonough, M A.]]
[[Category: Schofield, C J.]]
[[Category: Schofield, C J.]]
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[[Category: ankyrin repeat]]
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[[Category: Ankyrin repeat]]
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[[Category: beta-hydroxy asparagine]]
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[[Category: Beta-hydroxy asparagine]]
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[[Category: factor inhibiting hif]]
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[[Category: Factor inhibiting hif]]
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[[Category: transcription]]
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[[Category: Transcription]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:42:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:47:33 2008''
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Revision as of 11:42, 4 May 2008

Template:STRUCTURE 2qc9

Mouse Notch 1 Ankyrin Repeat Intracellular Domain


Overview

The stability and activity of hypoxia-inducible factor (HIF) are regulated by the post-translational hydroxylation of specific prolyl and asparaginyl residues. We show that the HIF asparaginyl hydroxylase, factor inhibiting HIF (FIH), also catalyzes hydroxylation of highly conserved asparaginyl residues within ankyrin repeat (AR) domains (ARDs) of endogenous Notch receptors. AR hydroxylation decreases the extent of ARD binding to FIH while not affecting signaling through the canonical Notch pathway. ARD proteins were found to efficiently compete with HIF for FIH-dependent hydroxylation. Crystallographic analyses of the hydroxylated Notch ARD (2.35A) and of Notch peptides bound to FIH (2.4-2.6A) reveal the stereochemistry of hydroxylation on the AR and imply that significant conformational changes are required in the ARD fold in order to enable hydroxylation at the FIH active site. We propose that ARD proteins function as natural inhibitors of FIH and that the hydroxylation status of these proteins provides another oxygen-dependent interface that modulates HIF signaling.

About this Structure

2QC9 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Asparaginyl hydroxylation of the Notch ankyrin repeat domain by factor inhibiting hypoxia-inducible factor., Coleman ML, McDonough MA, Hewitson KS, Coles C, Mecinovic J, Edelmann M, Cook KM, Cockman ME, Lancaster DE, Kessler BM, Oldham NJ, Ratcliffe PJ, Schofield CJ, J Biol Chem. 2007 Aug 17;282(33):24027-38. Epub 2007 Jun 15. PMID:17573339 Page seeded by OCA on Sun May 4 14:42:43 2008

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