1h2n: Difference between revisions
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Revision as of 16:21, 30 October 2007
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FACTOR INHIBITING HIF-1 ALPHA
OverviewOverview
The activity of the transcription factor hypoxia-inducible factor (HIF) is, regulated by oxygen-dependent hydroxylation. Under normoxic conditions, hydroxylation of proline residues triggers destruction of its, alpha-subunit while hydroxylation of Asn(803) in the C-terminal, transactivation domain of HIF-1 alpha (CAD) prevents its interaction with, p300. Here we report crystal structures of the asparagine hydroxylase, (factor-inhibiting HIF, FIH) complexed with Fe((II)), 2-oxoglutarate, cosubstrate, and CAD fragments, which reveal the structural basis of HIF, modification. CAD binding to FIH occurs via an induced fit process at two, distinct interaction sites. At the hydroxylation site CAD adopts a loop, conformation, contrasting with a helical conformation for the same, residues when ... [(full description)]
About this StructureAbout this Structure
1H2N is a [Single protein] structure of sequence from [Homo sapiens] with FE2, SO4 and AKG as [ligands]. Structure known Active Site: FEA. Full crystallographic information is available from [OCA].
ReferenceReference
Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alpha., Elkins JM, Hewitson KS, McNeill LA, Seibel JF, Schlemminger I, Pugh CW, Ratcliffe PJ, Schofield CJ, J Biol Chem. 2003 Jan 17;278(3):1802-6. Epub 2002 Nov 21. PMID:12446723
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