1iz3: Difference between revisions
New page: left|200px<br /> <applet load="1iz3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iz3, resolution 2.8Å" /> '''Dimeric structure of... |
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caption="1iz3, resolution 2.8Å" /> | caption="1iz3, resolution 2.8Å" /> | ||
'''Dimeric structure of FIH (Factor inhibiting HIF)'''<br /> | '''Dimeric structure of FIH (Factor inhibiting HIF)'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1IZ3 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 SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1IZ3 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=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IZ3 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: double beta-sheet helix]] | [[Category: double beta-sheet helix]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:04:41 2008'' | ||
Revision as of 17:04, 15 February 2008
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Dimeric structure of FIH (Factor inhibiting HIF)
OverviewOverview
The master switch of cellular hypoxia responses, hypoxia-inducible factor, 1 (HIF-1), is hydroxylated by factor inhibiting HIF-1 (FIH-1) at a, conserved asparagine residue under normoxia, which suppresses, transcriptional activity of HIF-1 by abrogating its interaction with, transcription coactivators. Here we report the crystal structure of human, FIH-1 at 2.8-A resolution. The structural core of FIH-1 consists of a, jellyroll-like beta-barrel containing the conserved ferrous-binding triad, residues, confirming that FIH-1 is a member of the, 2-oxoglutarate-dependent dioxygenase family. Except for the core structure, and triad residues, FIH-1 has many structural deviations from other family, members including N- and C-terminal insertions and various deletions in, the middle of the structure. The ferrous-binding triad region is highly, exposed to the solvent, which is connected to a prominent groove that may, bind to a helix near the hydroxylation site of HIF-1. The structure, which, is in a dimeric state, also reveals the putative von Hippel-Lindau-binding, site that is distinctive to the putative HIF-1-binding site, supporting, the formation of the ternary complex by FIH-1, HIF-1, and von, Hippel-Lindau. The unique environment of the active site and, cofactor-binding region revealed in the structure should allow design of, selective drugs that can be used in ischemic diseases to promote hypoxia, responses.
About this StructureAbout this Structure
1IZ3 is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Structure of human FIH-1 reveals a unique active site pocket and interaction sites for HIF-1 and von Hippel-Lindau., Lee C, Kim SJ, Jeong DG, Lee SM, Ryu SE, J Biol Chem. 2003 Feb 28;278(9):7558-63. Epub 2002 Dec 12. PMID:12482756
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