9h9t

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Current revision (08:28, 4 June 2025) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9h9t is ON HOLD until Paper Publication
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==Crystal structure of NEDD4 HECT domain in complex with covalent inhibitor==
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<StructureSection load='9h9t' size='340' side='right'caption='[[9h9t]], [[Resolution|resolution]] 2.17&Aring;' scene=''>
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Authors: Cecatiello, V., Maspero, E., Polo, S., Pasqualato, S.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9h9t]] is a 1 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=9H9T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9H9T FirstGlance]. <br>
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Description: Crystal structure of NEDD4 HECT domain in complex with covalent inhibitor
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.17&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1ITT:ethyl+4-[4-(2-chloranyl-5,6-dihydrobenzo[b][1]benzazepin-11-yl)butylamino]butanoate'>A1ITT</scene></td></tr>
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[[Category: Pasqualato, S]]
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9h9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9h9t OCA], [https://pdbe.org/9h9t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9h9t RCSB], [https://www.ebi.ac.uk/pdbsum/9h9t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9h9t ProSAT]</span></td></tr>
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[[Category: Polo, S]]
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</table>
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[[Category: Maspero, E]]
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== Function ==
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[[Category: Cecatiello, V]]
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[https://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>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Cecatiello V]]
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[[Category: Maspero E]]
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[[Category: Pasqualato S]]
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[[Category: Polo S]]

Current revision

Crystal structure of NEDD4 HECT domain in complex with covalent inhibitor

PDB ID 9h9t

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