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- | [[Image:1nj3.gif|left|200px]] | |
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- | {{Structure
| + | ==Structure and Ubiquitin Interactions of the Conserved NZF Domain of Npl4== |
- | |PDB= 1nj3 |SIZE=350|CAPTION= <scene name='initialview01'>1nj3</scene>
| + | <StructureSection load='1nj3' size='340' side='right'caption='[[1nj3]]' scene=''> |
- | |SITE= | + | == Structural highlights == |
- | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | + | <table><tr><td colspan='2'>[[1nj3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NJ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NJ3 FirstGlance]. <br> |
- | |ACTIVITY=
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
- | |GENE= Npl4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
- | |DOMAIN=
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nj3 OCA], [https://pdbe.org/1nj3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nj3 RCSB], [https://www.ebi.ac.uk/pdbsum/1nj3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nj3 ProSAT]</span></td></tr> |
- | |RELATEDENTRY=
| + | </table> |
- | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nj3 OCA], [http://www.ebi.ac.uk/pdbsum/1nj3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nj3 RCSB]</span>
| + | == Function == |
- | }}
| + | [https://www.uniprot.org/uniprot/NPL4_RAT NPL4_RAT] The ternary complex containing UFD1L, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1L-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope.<ref>PMID:10811609</ref> <ref>PMID:11781570</ref> <ref>PMID:11740563</ref> <ref>PMID:14636562</ref> <ref>PMID:12411482</ref> <ref>PMID:12644454</ref> |
- | | + | == Evolutionary Conservation == |
- | '''Structure and Ubiquitin Interactions of the Conserved NZF Domain of Npl4'''
| + | [[Image:Consurf_key_small.gif|200px|right]] |
- | | + | Check<jmol> |
- | | + | <jmolCheckbox> |
- | ==Overview== | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nj/1nj3_consurf.spt"</scriptWhenChecked> |
- | Ubiquitylated proteins are directed into a large number of different cellular pathways through interactions with effector proteins that contain conserved ubiquitin binding motifs. Here, we report the solution structure and ubiquitin binding properties of one such motif, the Npl4 zinc finger or RanBP2/Nup358 zinc finger (NZF) domain. Npl4 NZF forms a compact module composed of four antiparallel beta-strands linked by three ordered loops. A single zinc ion is coordinated by four conserved cysteines from the first and third loops, which form two rubredoxin knuckles. Npl4 NZF binds specifically, but weakly, to free ubiquitin using a conserved 13TF14 dipeptide to interact with the "Ile-44" surface of ubiquitin. Our studies reveal the structure of this versatile class of protein binding domains and provide a means for identifying the subset of NZF domains likely to bind ubiquitin.
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
- | | + | <text>to colour the structure by Evolutionary Conservation</text> |
- | ==About this Structure== | + | </jmolCheckbox> |
- | 1NJ3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NJ3 OCA].
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1nj3 ConSurf]. |
- | | + | <div style="clear:both"></div> |
- | ==Reference== | + | == References == |
- | Structure and ubiquitin interactions of the conserved zinc finger domain of Npl4., Wang B, Alam SL, Meyer HH, Payne M, Stemmler TL, Davis DR, Sundquist WI, J Biol Chem. 2003 May 30;278(22):20225-34. Epub 2003 Mar 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12644454 12644454]
| + | <references/> |
| + | __TOC__ |
| + | </StructureSection> |
| + | [[Category: Large Structures]] |
| [[Category: Rattus norvegicus]] | | [[Category: Rattus norvegicus]] |
- | [[Category: Single protein]]
| + | [[Category: Alam SL]] |
- | [[Category: Alam, S L.]] | + | [[Category: Davis DR]] |
- | [[Category: Davis, D R.]] | + | [[Category: Meyer HH]] |
- | [[Category: Meyer, H H.]] | + | [[Category: Payne M]] |
- | [[Category: Payne, M.]] | + | [[Category: Stemmler TL]] |
- | [[Category: Stemmler, T L.]] | + | [[Category: Sundquist WI]] |
- | [[Category: Sundquist, W I.]] | + | [[Category: Wang B]] |
- | [[Category: Wang, B.]] | + | |
- | [[Category: beta-ribbon]]
| + | |
- | [[Category: npl4]]
| + | |
- | [[Category: nzf domain]]
| + | |
- | [[Category: rubredoxin knuckle]]
| + | |
- | [[Category: ubiquitin]]
| + | |
- | [[Category: zinc-finger]]
| + | |
- | | + | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:31:04 2008''
| + | |
| Structural highlights
Function
NPL4_RAT The ternary complex containing UFD1L, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1L-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope.[1] [2] [3] [4] [5] [6]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Meyer HH, Shorter JG, Seemann J, Pappin D, Warren G. A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways. EMBO J. 2000 May 15;19(10):2181-92. PMID:10811609 doi:http://dx.doi.org/10.1093/emboj/19.10.2181
- ↑ Hetzer M, Meyer HH, Walther TC, Bilbao-Cortes D, Warren G, Mattaj IW. Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly. Nat Cell Biol. 2001 Dec;3(12):1086-91. PMID:11781570 doi:http://dx.doi.org/10.1038/ncb1201-1086
- ↑ Ye Y, Meyer HH, Rapoport TA. The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature. 2001 Dec 6;414(6864):652-6. PMID:11740563 doi:http://dx.doi.org/10.1038/414652a
- ↑ Cao K, Nakajima R, Meyer HH, Zheng Y. The AAA-ATPase Cdc48/p97 regulates spindle disassembly at the end of mitosis. Cell. 2003 Oct 31;115(3):355-67. PMID:14636562
- ↑ Meyer HH, Wang Y, Warren G. Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4. EMBO J. 2002 Nov 1;21(21):5645-52. PMID:12411482
- ↑ Wang B, Alam SL, Meyer HH, Payne M, Stemmler TL, Davis DR, Sundquist WI. Structure and ubiquitin interactions of the conserved zinc finger domain of Npl4. J Biol Chem. 2003 May 30;278(22):20225-34. Epub 2003 Mar 18. PMID:12644454 doi:10.1074/jbc.M300459200
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