2zgd
From Proteopedia
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|PDB= 2zgd |SIZE=350|CAPTION= <scene name='initialview01'>2zgd</scene>, resolution 1.900Å | |PDB= 2zgd |SIZE=350|CAPTION= <scene name='initialview01'>2zgd</scene>, resolution 1.900Å | ||
|SITE= <scene name='pdbsite=AC1:Cd+Binding+Site+For+Residue+A+410'>AC1</scene>, <scene name='pdbsite=AC2:Cd+Binding+Site+For+Residue+A+411'>AC2</scene>, <scene name='pdbsite=AC3:Cd+Binding+Site+For+Residue+A+412'>AC3</scene>, <scene name='pdbsite=AC4:Cd+Binding+Site+For+Residue+A+413'>AC4</scene>, <scene name='pdbsite=AC5:Cd+Binding+Site+For+Residue+A+414'>AC5</scene>, <scene name='pdbsite=AC6:Cl+Binding+Site+For+Residue+A+415'>AC6</scene> and <scene name='pdbsite=AC7:Cl+Binding+Site+For+Residue+A+416'>AC7</scene> | |SITE= <scene name='pdbsite=AC1:Cd+Binding+Site+For+Residue+A+410'>AC1</scene>, <scene name='pdbsite=AC2:Cd+Binding+Site+For+Residue+A+411'>AC2</scene>, <scene name='pdbsite=AC3:Cd+Binding+Site+For+Residue+A+412'>AC3</scene>, <scene name='pdbsite=AC4:Cd+Binding+Site+For+Residue+A+413'>AC4</scene>, <scene name='pdbsite=AC5:Cd+Binding+Site+For+Residue+A+414'>AC5</scene>, <scene name='pdbsite=AC6:Cl+Binding+Site+For+Residue+A+415'>AC6</scene> and <scene name='pdbsite=AC7:Cl+Binding+Site+For+Residue+A+416'>AC7</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> | + | |LIGAND= <scene name='pdbligand=AHB:BETA-HYDROXYASPARAGINE'>AHB</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2zgg|2ZGG]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zgd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zgd OCA], [http://www.ebi.ac.uk/pdbsum/2zgd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2zgd RCSB]</span> | ||
}} | }} | ||
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[[Category: McDonough, M A.]] | [[Category: McDonough, M A.]] | ||
[[Category: Schofield, C J.]] | [[Category: Schofield, C J.]] | ||
| - | [[Category: CD]] | ||
| - | [[Category: CL]] | ||
[[Category: ankyrin repeat]] | [[Category: ankyrin repeat]] | ||
[[Category: de novo protein]] | [[Category: de novo protein]] | ||
[[Category: hydroxylated]] | [[Category: hydroxylated]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:20:58 2008'' |
Revision as of 02:21, 31 March 2008
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| , resolution 1.900Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , and | ||||||
| Ligands: | , , | ||||||
| Related: | 2ZGG
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Asn-hydroxylation stabilises the ankyrin repeat domain fold
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
2ZGD is a Single protein structure of sequence from [1]. 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 Mon Mar 31 05:20:58 2008
