This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2wa3
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2wa3]] is a 1 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=2WA3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WA3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2wa3]] is a 1 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=2WA3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WA3 FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A29:2-(3-HYDROXYPHENYL)-2-OXO-ETHANOIC+ACID'>A29</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A29:2-(3-HYDROXYPHENYL)-2-OXO-ETHANOIC+ACID'>A29</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wa4|2wa4]], [[1mze|1mze]], [[2w0x|2w0x]], [[2cgn|2cgn]], [[1mzf|1mzf]], [[1h2n|1h2n]], [[1yci|1yci]], [[2cgo|2cgo]], [[1h2k|1h2k]], [[1iz3|1iz3]], [[1h2l|1h2l]], [[1h2m|1h2m]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wa4|2wa4]], [[1mze|1mze]], [[2w0x|2w0x]], [[2cgn|2cgn]], [[1mzf|1mzf]], [[1h2n|1h2n]], [[1yci|1yci]], [[2cgo|2cgo]], [[1h2k|1h2k]], [[1iz3|1iz3]], [[1h2l|1h2l]], [[1h2m|1h2m]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptide-aspartate_beta-dioxygenase Peptide-aspartate beta-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.16 1.14.11.16] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptide-aspartate_beta-dioxygenase Peptide-aspartate beta-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.16 1.14.11.16] </span></td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wa3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wa3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wa3 RCSB], [http://www.ebi.ac.uk/pdbsum/2wa3 PDBsum]</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=2wa3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wa3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wa3 RCSB], [http://www.ebi.ac.uk/pdbsum/2wa3 PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == 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> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 35: | Line 37: | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Peptide-aspartate beta-dioxygenase]] | [[Category: Peptide-aspartate beta-dioxygenase]] | ||
| - | [[Category: Clifton, I J | + | [[Category: Clifton, I J]] |
| - | [[Category: Conejo-Garcia, A | + | [[Category: Conejo-Garcia, A]] |
| - | [[Category: Lienard, B M.R | + | [[Category: Lienard, B M.R]] |
| - | [[Category: Mcdonough, M A | + | [[Category: Mcdonough, M A]] |
| - | [[Category: Schofield, C J | + | [[Category: Schofield, C J]] |
[[Category: Dioxygenase]] | [[Category: Dioxygenase]] | ||
[[Category: Hydroxylase]] | [[Category: Hydroxylase]] | ||
Revision as of 11:51, 25 December 2014
FACTOR INHIBITING HIF-1 ALPHA WITH 2-(3-HYDROXYPHENYL)-2-OXOACETIC ACID
| |||||||||||
