1h2k
From Proteopedia
(New page: 200px<br /> <applet load="1h2k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h2k, resolution 2.15Å" /> '''FACTOR INHIBITING H...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1H2K is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with FE2, SO4 and OGA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H2K OCA]]. | + | 1H2K is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with FE2, SO4 and OGA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Structure known Active Site: FE1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H2K OCA]]. |
==Reference== | ==Reference== | ||
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[[Category: transcription]] | [[Category: transcription]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:23:59 2007'' |
Revision as of 10:19, 30 October 2007
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FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH HIF-1 ALPHA FRAGMENT PEPTIDE
Overview
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 Structure
1H2K is a [Protein complex] structure of sequences from [Homo sapiens] with FE2, SO4 and OGA as [ligands]. Structure known Active Site: FE1. Full crystallographic information is available from [OCA].
Reference
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
Page seeded by OCA on Tue Oct 30 12:23:59 2007
Categories: Homo sapiens | Protein complex | Elkins, J.M. | Hewitson, K.S. | Mcneill, L.A. | Schlemminger, I. | Schofield, C.J. | Seibel, J.F. | FE2 | OGA | SO4 | 2-oxoglutarate | Asparaginyl hydroxylase | Dsbh | Fih | Hif | Hypoxia | Oxygenase | Phosphorylation | Transcription
