2qc9
From Proteopedia
(New page: 200px<br /><applet load="2qc9" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qc9, resolution 2.350Å" /> '''Mouse Notch 1 Ankyr...) |
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| - | [[Image:2qc9.jpg|left|200px]] | + | [[Image:2qc9.jpg|left|200px]] |
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| - | '''Mouse Notch 1 Ankyrin Repeat Intracellular Domain''' | + | {{Structure |
| + | |PDB= 2qc9 |SIZE=350|CAPTION= <scene name='initialview01'>2qc9</scene>, resolution 2.350Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= Notch1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | }} | ||
| + | |||
| + | '''Mouse Notch 1 Ankyrin Repeat Intracellular Domain''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2QC9 is a [ | + | 2QC9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QC9 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17573339 17573339] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transcription]] | [[Category: transcription]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:24:14 2008'' |
Revision as of 16:24, 20 March 2008
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| , resolution 2.350Å | |||||||
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| Gene: | Notch1 (Mus musculus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 18:24:14 2008
