2m3o

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(New page: '''Unreleased structure''' The entry 2m3o is ON HOLD Authors: Bobby, R., Medini, K., Neudecker, P., Lee, V., MacDonald, F.J., Brimble, M.A., Lott, J., Dingley, A.J. Description: Struct...)
Current revision (06:58, 1 May 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 2m3o is ON HOLD
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==Structure and dynamics of a human Nedd4 WW domain-ENaC complex==
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<StructureSection load='2m3o' size='340' side='right'caption='[[2m3o]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2m3o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M3O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M3O FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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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=2m3o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m3o OCA], [https://pdbe.org/2m3o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m3o RCSB], [https://www.ebi.ac.uk/pdbsum/2m3o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m3o ProSAT]</span></td></tr>
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</table>
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== Function ==
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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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Authors: Bobby, R., Medini, K., Neudecker, P., Lee, V., MacDonald, F.J., Brimble, M.A., Lott, J., Dingley, A.J.
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==See Also==
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*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
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Description: Structure and dynamics of a human Nedd4 WW domain-ENaC complex
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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: Bobby R]]
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[[Category: Brimble MA]]
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[[Category: Dingley AJ]]
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[[Category: Lee V]]
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[[Category: Lott J]]
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[[Category: MacDonald FJ]]
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[[Category: Medini K]]
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[[Category: Neudecker P]]

Current revision

Structure and dynamics of a human Nedd4 WW domain-ENaC complex

PDB ID 2m3o

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