1wr7: Difference between revisions
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==Solution structure of the third WW domain of Nedd4-2== | ==Solution structure of the third WW domain of Nedd4-2== | ||
<StructureSection load='1wr7' size='340' side='right'caption='[[1wr7 | <StructureSection load='1wr7' size='340' side='right'caption='[[1wr7]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1wr7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1wr7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WR7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WR7 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1wr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wr7 OCA], [https://pdbe.org/1wr7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wr7 RCSB], [https://www.ebi.ac.uk/pdbsum/1wr7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wr7 ProSAT]</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=1wr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wr7 OCA], [https://pdbe.org/1wr7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wr7 RCSB], [https://www.ebi.ac.uk/pdbsum/1wr7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wr7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/NED4L_MOUSE NED4L_MOUSE] 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. Inhibits TGF-beta signaling by triggering SMAD2 and TGFBR1 ubiquitination and proteasome-dependent degradation. Promotes ubiquitination and internalization of various plasma membrane channels such as ENaC, Nav1.2, Nav1.3, Nav1.5, Nav1.7, Nav1.8, Kv1.3, EAAT1 or CLC5. Promotes ubiquitination and degradation of SGK1 and TNK2.<ref>PMID:11149908</ref> <ref>PMID:12424229</ref> <ref>PMID:11742982</ref> <ref>PMID:11244092</ref> <ref>PMID:15123669</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: Booker | [[Category: Booker GW]] | ||
[[Category: Kowalski | [[Category: Kowalski K]] | ||
[[Category: Merkel | [[Category: Merkel AL]] | ||
Latest revision as of 16:47, 9 May 2024
Solution structure of the third WW domain of Nedd4-2Solution structure of the third WW domain of Nedd4-2
Structural highlights
FunctionNED4L_MOUSE 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. Inhibits TGF-beta signaling by triggering SMAD2 and TGFBR1 ubiquitination and proteasome-dependent degradation. Promotes ubiquitination and internalization of various plasma membrane channels such as ENaC, Nav1.2, Nav1.3, Nav1.5, Nav1.7, Nav1.8, Kv1.3, EAAT1 or CLC5. Promotes ubiquitination and degradation of SGK1 and TNK2.[1] [2] [3] [4] [5] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See AlsoReferences
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