4z1v

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
'''Unreleased structure'''
+
==Structure of Factor Inhibiting HIF (FIH) in complex with Fe, NO, and NOG==
-
 
+
<StructureSection load='4z1v' size='340' side='right' caption='[[4z1v]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
-
The entry 4z1v is ON HOLD until Paper Publication
+
== Structural highlights ==
-
 
+
<table><tr><td colspan='2'>[[4z1v]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z1V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Z1V FirstGlance]. <br>
-
Authors: Taabazuing, C.Y., Garman, S.C., Knapp, M.J.
+
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=NO:NITRIC+OXIDE'>NO</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-
 
+
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4z2w|4z2w]]</td></tr>
-
Description:
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4z1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z1v OCA], [http://pdbe.org/4z1v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4z1v RCSB], [http://www.ebi.ac.uk/pdbsum/4z1v PDBsum]</span></td></tr>
-
[[Category: Unreleased Structures]]
+
</table>
-
[[Category: Taabazuing, C.Y]]
+
== Function ==
-
[[Category: Knapp, M.J]]
+
[[http://www.uniprot.org/uniprot/HIF1N_HUMAN HIF1N_HUMAN]] Hydroxylates HIF-1 alpha at 'Asp-803' in the C-terminal transactivation domain (CAD). Functions as an oxygen sensor and, under normoxic conditions, the hydroxylation prevents interaction of HIF-1 with transcriptional coactivators including Cbp/p300-interacting transactivator. Involved in transcriptional repression through interaction with HIF1A, VHL and histone deacetylases. Hydroxylates specific Asn residues within ankyrin repeat domains (ARD) of NFKB1, NFKBIA, NOTCH1, ASB4, PPP1R12A and several other ARD-containing proteins. Also hydroxylates Asp and His residues within ARDs of ANK1 and TNKS2, respectively. Negatively regulates NOTCH1 activity, accelerating myogenic differentiation. Positively regulates ASB4 activity, promoting vascular differentiation.<ref>PMID:12080085</ref> <ref>PMID:12042299</ref> <ref>PMID:17003112</ref> <ref>PMID:18299578</ref> <ref>PMID:19245366</ref> <ref>PMID:17573339</ref> <ref>PMID:21251231</ref> <ref>PMID:21177872</ref>
-
[[Category: Garman, S.C]]
+
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Garman, S C]]
 +
[[Category: Knapp, M J]]
 +
[[Category: Taabazuing, C Y]]
 +
[[Category: Factor inhibiting hif]]
 +
[[Category: Hydroxylase]]
 +
[[Category: Hypoxia inducible factor]]
 +
[[Category: Oxidoreductase]]
 +
[[Category: Oxygen sensing]]

Revision as of 20:24, 13 January 2016

Structure of Factor Inhibiting HIF (FIH) in complex with Fe, NO, and NOG

4z1v, resolution 2.10Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4z1v"
Personal tools