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5c91
From Proteopedia
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| - | ''' | + | ==NEDD4 HECT with covalently bound indole-based inhibitor== |
| - | + | <StructureSection load='5c91' size='340' side='right' caption='[[5c91]], [[Resolution|resolution]] 2.44Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5c91]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C91 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C91 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4YU:METHYL+(2E)-4-{[(5-METHOXY-1,2-DIMETHYL-1H-INDOL-3-YL)CARBONYL]AMINO}BUT-2-ENOATE'>4YU</scene></td></tr> | |
| - | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xbf|2xbf]], [[2xbb|2xbb]]</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=5c91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c91 OCA], [http://pdbe.org/5c91 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c91 RCSB], [http://www.ebi.ac.uk/pdbsum/5c91 PDBsum]</span></td></tr> | |
| - | [[ | + | </table> |
| - | [[ | + | == Function == |
| - | [[ | + | [[http://www.uniprot.org/uniprot/NEDD4_HUMAN NEDD4_HUMAN]] E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Involved in the pathway leading to the degradation of VEGFR-2/KDFR, independently of its ubiquitin-ligase activity. Monoubiquitinates IGF1R at multiple sites, thus leading to receptor internalization and degradation in lysosomes. Ubiquitinates FGFR1, leading to receptor internalization and degradation in lysosomes. According to PubMed:18562292 the direct link between NEDD4 and PTEN regulation through polyubiquitination described in PubMed:17218260 is questionable. Involved in ubiquitination of ERBB4 intracellular domain E4ICD. Involved in the budding of many viruses. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. Ubiquitinates TNK2 and regulates EGF-induced degradation of EGFR and TNF2.<ref>PMID:17218260</ref> <ref>PMID:18562292</ref> <ref>PMID:20086093</ref> <ref>PMID:21765395</ref> <ref>PMID:21399620</ref> |
| - | [[ | + | == References == |
| - | [[ | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Kathman, S]] | [[Category: Kathman, S]] | ||
| + | [[Category: Rosenzweig, A C]] | ||
| + | [[Category: Smith, A T]] | ||
| + | [[Category: Span, I]] | ||
| + | [[Category: Statsyuk, A V]] | ||
| + | [[Category: Hect]] | ||
| + | [[Category: Inhibitor]] | ||
| + | [[Category: Ligase]] | ||
| + | [[Category: Ligase-ligase inhibitor complex]] | ||
| + | [[Category: Nedd4]] | ||
Revision as of 14:43, 30 September 2015
NEDD4 HECT with covalently bound indole-based inhibitor
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