4nr1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (17:01, 20 September 2023) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
==Factor inhibiting HIF-1 alpha in complex with consensus ankyrin repeat domain-(d)allyl-GLY peptide==
==Factor inhibiting HIF-1 alpha in complex with consensus ankyrin repeat domain-(d)allyl-GLY peptide==
-
<StructureSection load='4nr1' size='340' side='right' caption='[[4nr1]], [[Resolution|resolution]] 2.68&Aring;' scene=''>
+
<StructureSection load='4nr1' size='340' side='right'caption='[[4nr1]], [[Resolution|resolution]] 2.68&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4nr1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NR1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NR1 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4nr1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NR1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NR1 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.68&#8491;</td></tr>
-
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DYL:(2R)-2-AMINOPENT-4-ENOIC+ACID'>DYL</scene></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DYL:(2R)-2-AMINOPENT-4-ENOIC+ACID'>DYL</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4jaa|4jaa]]</td></tr>
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4nr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nr1 OCA], [https://pdbe.org/4nr1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nr1 RCSB], [https://www.ebi.ac.uk/pdbsum/4nr1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nr1 ProSAT]</span></td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hypoxia-inducible_factor-asparagine_dioxygenase Hypoxia-inducible factor-asparagine dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.30 1.14.11.30] </span></td></tr>
+
-
<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=4nr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nr1 OCA], [http://pdbe.org/4nr1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nr1 RCSB], [http://www.ebi.ac.uk/pdbsum/4nr1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nr1 ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[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>
+
[https://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>
==See Also==
==See Also==
Line 19: Line 17:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Hypoxia-inducible factor-asparagine dioxygenase]]
+
[[Category: Homo sapiens]]
-
[[Category: McDonough, M A]]
+
[[Category: Large Structures]]
-
[[Category: Schofield, C J]]
+
[[Category: McDonough MA]]
-
[[Category: Scotti, J S]]
+
[[Category: Schofield CJ]]
-
[[Category: Activator-inhibitor]]
+
[[Category: Scotti JS]]
-
[[Category: Ard]]
+
-
[[Category: Asparaginyl/aspartyl hydroxylase]]
+
-
[[Category: Beta-hydroxylation]]
+
-
[[Category: Dioxygenase]]
+
-
[[Category: Dna-binding]]
+
-
[[Category: Dsbh]]
+
-
[[Category: Epigenetic regulation]]
+
-
[[Category: Facial triad]]
+
-
[[Category: Helix-loop-helix-beta]]
+
-
[[Category: Metal-binding]]
+
-
[[Category: On-heme]]
+
-
[[Category: Oxidoreductase]]
+
-
[[Category: Oxidoreductase-peptide complex]]
+
-
[[Category: Oxygenase]]
+
-
[[Category: Signaling]]
+
-
[[Category: Transcription]]
+

Current revision

Factor inhibiting HIF-1 alpha in complex with consensus ankyrin repeat domain-(d)allyl-GLY peptide

PDB ID 4nr1

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/4nr1"
Personal tools