1yci

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[[Image:1yci.gif|left|200px]]<br /><applet load="1yci" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1yci.gif|left|200px]]
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caption="1yci, resolution 2.70&Aring;" />
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'''Factor inhibiting HIF-1 alpha in complex with N-(carboxycarbonyl)-D-phenylalanine'''<br />
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{{Structure
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|PDB= 1yci |SIZE=350|CAPTION= <scene name='initialview01'>1yci</scene>, resolution 2.70&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=NDF:N-(CARBOXYCARBONYL)-D-PHENYLALANINE'>NDF</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Peptide-aspartate_beta-dioxygenase Peptide-aspartate beta-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.16 1.14.11.16]
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|GENE= HIF1AN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Factor inhibiting HIF-1 alpha in complex with N-(carboxycarbonyl)-D-phenylalanine'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1YCI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=FE2:'>FE2</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=NDF:'>NDF</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Peptide-aspartate_beta-dioxygenase Peptide-aspartate beta-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.16 1.14.11.16] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YCI OCA].
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1YCI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YCI OCA].
==Reference==
==Reference==
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Selective inhibition of factor inhibiting hypoxia-inducible factor., McDonough MA, McNeill LA, Tilliet M, Papamicael CA, Chen QY, Banerji B, Hewitson KS, Schofield CJ, J Am Chem Soc. 2005 Jun 1;127(21):7680-1. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15913349 15913349]
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Selective inhibition of factor inhibiting hypoxia-inducible factor., McDonough MA, McNeill LA, Tilliet M, Papamicael CA, Chen QY, Banerji B, Hewitson KS, Schofield CJ, J Am Chem Soc. 2005 Jun 1;127(21):7680-1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15913349 15913349]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Peptide-aspartate beta-dioxygenase]]
[[Category: Peptide-aspartate beta-dioxygenase]]
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[[Category: transcription]]
[[Category: transcription]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:03:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:21:08 2008''

Revision as of 13:21, 20 March 2008

Image:1yci.gif


PDB ID 1yci

Drag the structure with the mouse to rotate
, resolution 2.70Å
Ligands: , and
Gene: HIF1AN (Homo sapiens)
Activity: Peptide-aspartate beta-dioxygenase, with EC number 1.14.11.16
Coordinates: save as pdb, mmCIF, xml



Factor inhibiting HIF-1 alpha in complex with N-(carboxycarbonyl)-D-phenylalanine


Overview

A set of four non-heme iron(II) and 2-oxoglutarate-dependent enzymes catalyze the post-translational modification of a transcription factor, hypoxia inducible factor (HIF), that mediates the hypoxic response in animals. Hydroxylation of HIF both causes its degradation and limits its activity. We describe how the use of structural data coupled to solid-phase synthesis led to the discovery of a selective inhibitor of one of the HIF hydroxylases. The inhibitor N-oxalyl-d-phenylalanine was shown to inhibit the HIF asparaginyl hydroxylase (FIH) but not a HIF prolyl hydroxylase. A crystal structure of the inhibitor complexed to FIH reveals that it binds in the 2OG and, likely, in the dioxygen binding site. The results will help to enable the modulation of the hypoxic response for the up-regulation of specific genes of biomedical importance, such as erythropoietin and vascular endothelial growth factor.

About this Structure

1YCI is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Selective inhibition of factor inhibiting hypoxia-inducible factor., McDonough MA, McNeill LA, Tilliet M, Papamicael CA, Chen QY, Banerji B, Hewitson KS, Schofield CJ, J Am Chem Soc. 2005 Jun 1;127(21):7680-1. PMID:15913349

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