4b7e

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:44, 20 December 2023) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
 +
==FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH CONSENSUS ANKYRIN REPEAT DOMAIN-LEU PEPTIDE (20-MER)==
==FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH CONSENSUS ANKYRIN REPEAT DOMAIN-LEU PEPTIDE (20-MER)==
-
<StructureSection load='4b7e' size='340' side='right' caption='[[4b7e]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+
<StructureSection load='4b7e' size='340' side='right'caption='[[4b7e]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4b7e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B7E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B7E FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4b7e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B7E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B7E FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1h2k|1h2k]], [[1h2l|1h2l]], [[1h2m|1h2m]], [[1h2n|1h2n]], [[1iz3|1iz3]], [[1mze|1mze]], [[1mzf|1mzf]], [[1yci|1yci]], [[2cgn|2cgn]], [[2cgo|2cgo]], [[2w0x|2w0x]], [[2wa3|2wa3]], [[2wa4|2wa4]], [[2xum|2xum]], [[2y0i|2y0i]], [[2yc0|2yc0]], [[2yde|2yde]], [[4ai8|4ai8]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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='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=4b7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b7e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b7e RCSB], [http://www.ebi.ac.uk/pdbsum/4b7e PDBsum]</span></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=4b7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b7e OCA], [https://pdbe.org/4b7e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b7e RCSB], [https://www.ebi.ac.uk/pdbsum/4b7e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b7e 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>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 17: Line 18:
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
 +
<div class="pdbe-citations 4b7e" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
*[[Factor inhibiting HIF|Factor inhibiting HIF]]
*[[Factor inhibiting HIF|Factor inhibiting HIF]]
 +
*[[Hypoxia-Inducible factor 1 alpha inhibitor|Hypoxia-Inducible factor 1 alpha inhibitor]]
== References ==
== References ==
<references/>
<references/>
Line 25: Line 28:
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Chowdhury, R]]
+
[[Category: Large Structures]]
-
[[Category: Ge, W]]
+
[[Category: Synthetic construct]]
-
[[Category: Schofield, C J]]
+
[[Category: Chowdhury R]]
-
[[Category: 2-oxoglutarate]]
+
[[Category: Ge W]]
-
[[Category: Ard]]
+
[[Category: Schofield CJ]]
-
[[Category: Asparaginyl/ aspartyl hydroxylase]]
+
-
[[Category: Beta-hydroxylation]]
+
-
[[Category: Dioxygenase]]
+
-
[[Category: Dna-binding]]
+
-
[[Category: Dsbh]]
+
-
[[Category: Facial triad]]
+
-
[[Category: Helix-loop-helix-beta]]
+
-
[[Category: Iron]]
+
-
[[Category: Metal-binding]]
+
-
[[Category: Non-heme]]
+
-
[[Category: Oxidoreductase]]
+
-
[[Category: Oxidoreductase-peptide complex]]
+
-
[[Category: Oxygenase]]
+
-
[[Category: Signaling]]
+
-
[[Category: Transcription]]
+
-
[[Category: Transcription activator/inhibitor]]
+
-
[[Category: Transcription and epigenetic regulation]]
+

Current revision

FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH CONSENSUS ANKYRIN REPEAT DOMAIN-LEU PEPTIDE (20-MER)

PDB ID 4b7e

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/4b7e"
Personal tools