From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1iz3.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:1iz3.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1iz3| PDB=1iz3 | SCENE= }} | | {{STRUCTURE_1iz3| PDB=1iz3 | SCENE= }} |
| | | | |
| - | '''Dimeric structure of FIH (Factor inhibiting HIF)'''
| + | ===Dimeric structure of FIH (Factor inhibiting HIF)=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | 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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_12482756}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12482756 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_12482756}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 28: |
Line 32: |
| | [[Category: Ryu, S E.]] | | [[Category: Ryu, S E.]] |
| | [[Category: Double beta-sheet helix]] | | [[Category: Double beta-sheet helix]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:36:29 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 14:15:09 2008'' |
Revision as of 11:15, 1 July 2008
Template:STRUCTURE 1iz3
Dimeric structure of FIH (Factor inhibiting HIF)
Template:ABSTRACT PUBMED 12482756
About this Structure
1IZ3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Tue Jul 1 14:15:09 2008
