2zgd

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[[Image:2zgd.jpg|left|200px]]<br /><applet load="2zgd" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2zgd.jpg|left|200px]]
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caption="2zgd, resolution 1.900&Aring;" />
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'''Asn-hydroxylation stabilises the ankyrin repeat domain fold'''<br />
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{{Structure
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|PDB= 2zgd |SIZE=350|CAPTION= <scene name='initialview01'>2zgd</scene>, resolution 1.900&Aring;
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|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>
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|LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''Asn-hydroxylation stabilises the ankyrin repeat domain fold'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2ZGD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=CD:'>CD</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <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>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZGD OCA].
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2ZGD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZGD OCA].
==Reference==
==Reference==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=17573339 17573339]
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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: Single protein]]
[[Category: Single protein]]
[[Category: McDonough, M A.]]
[[Category: McDonough, M A.]]
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[[Category: hydroxylated]]
[[Category: hydroxylated]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:01:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:54:12 2008''

Revision as of 16:54, 20 March 2008

Image:2zgd.jpg


PDB ID 2zgd

Drag the structure with the mouse to rotate
, resolution 1.900Å
Sites: , , , , , and
Ligands: and
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

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