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| | <StructureSection load='1yx5' size='340' side='right'caption='[[1yx5]], [[NMR_Ensembles_of_Models | 18 NMR models]]' scene=''> | | <StructureSection load='1yx5' size='340' side='right'caption='[[1yx5]], [[NMR_Ensembles_of_Models | 18 NMR models]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1yx5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YX5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1YX5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1yx5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YX5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YX5 FirstGlance]. <br> |
| | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1d3z|1d3z]], [[1tbe|1tbe]], [[1yx4|1yx4]], [[1yx6|1yx6]]</div></td></tr> | | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1d3z|1d3z]], [[1tbe|1tbe]], [[1yx4|1yx4]], [[1yx6|1yx6]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PSMD4, MCB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PSMD4, MCB1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1yx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yx5 OCA], [http://pdbe.org/1yx5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yx5 RCSB], [http://www.ebi.ac.uk/pdbsum/1yx5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1yx5 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=1yx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yx5 OCA], [https://pdbe.org/1yx5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yx5 RCSB], [https://www.ebi.ac.uk/pdbsum/1yx5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yx5 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PSD4_HUMAN PSD4_HUMAN]] Guanine nucleotide exchange factor for ARF6 and ARL14/ARF7. Through ARL14 activation, controls the movement of MHC class II-containing vesicles along the actin cytoskeleton in dendritic cells. Involved in membrane recycling. Interacts with several phosphatidylinositol phosphate species, including phosphatidylinositol 3,4-bisphosphate, phosphatidylinositol 3,5-bisphosphate and phosphatidylinositol 4,5-bisphosphate.<ref>PMID:12082148</ref> <ref>PMID:21458045</ref> | + | [[https://www.uniprot.org/uniprot/PSD4_HUMAN PSD4_HUMAN]] Guanine nucleotide exchange factor for ARF6 and ARL14/ARF7. Through ARL14 activation, controls the movement of MHC class II-containing vesicles along the actin cytoskeleton in dendritic cells. Involved in membrane recycling. Interacts with several phosphatidylinositol phosphate species, including phosphatidylinositol 3,4-bisphosphate, phosphatidylinositol 3,5-bisphosphate and phosphatidylinositol 4,5-bisphosphate.<ref>PMID:12082148</ref> <ref>PMID:21458045</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| | *[[Proteasome 3D structures|Proteasome 3D structures]] | | *[[Proteasome 3D structures|Proteasome 3D structures]] |
| - | *[[Ubiquitin|Ubiquitin]] | + | *[[3D structures of ubiquitin|3D structures of ubiquitin]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| Structural highlights
Function
[PSD4_HUMAN] Guanine nucleotide exchange factor for ARF6 and ARL14/ARF7. Through ARL14 activation, controls the movement of MHC class II-containing vesicles along the actin cytoskeleton in dendritic cells. Involved in membrane recycling. Interacts with several phosphatidylinositol phosphate species, including phosphatidylinositol 3,4-bisphosphate, phosphatidylinositol 3,5-bisphosphate and phosphatidylinositol 4,5-bisphosphate.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Ubiquitin is a key regulatory molecule in diverse cellular events. How cells determine the outcome of ubiquitylation remains unclear; however, a likely determinant is the specificity of ubiquitin receptor proteins for polyubiquitin chains of certain length and linkage. Proteasome subunit S5a contains two ubiquitin-interacting motifs (UIMs) through which it recruits ubiquitylated substrates to the proteasome for their degradation. Here, we report the structure of S5a (196-306) alone and complexed with two monoubiquitin molecules. This construct contains the two UIMs of S5a and we reveal their different ubiquitin-binding mechanisms and provide a rationale for their unique specificities for different ubiquitin-like domains. Furthermore, we provide direct evidence that S5a (196-306) binds either K63-linked or K48-linked polyubiquitin, and in both cases prefers longer chains. On the basis of these results we present a model for how S5a and other ubiquitin-binding proteins recognize polyubiquitin.
Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition.,Wang Q, Young P, Walters KJ J Mol Biol. 2005 May 6;348(3):727-39. PMID:15826667[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Derrien V, Couillault C, Franco M, Martineau S, Montcourrier P, Houlgatte R, Chavrier P. A conserved C-terminal domain of EFA6-family ARF6-guanine nucleotide exchange factors induces lengthening of microvilli-like membrane protrusions. J Cell Sci. 2002 Jul 15;115(Pt 14):2867-79. PMID:12082148
- ↑ Paul P, van den Hoorn T, Jongsma ML, Bakker MJ, Hengeveld R, Janssen L, Cresswell P, Egan DA, van Ham M, Ten Brinke A, Ovaa H, Beijersbergen RL, Kuijl C, Neefjes J. A Genome-wide multidimensional RNAi screen reveals pathways controlling MHC class II antigen presentation. Cell. 2011 Apr 15;145(2):268-83. doi: 10.1016/j.cell.2011.03.023. Epub 2011 Mar, 31. PMID:21458045 doi:http://dx.doi.org/10.1016/j.cell.2011.03.023
- ↑ Wang Q, Young P, Walters KJ. Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition. J Mol Biol. 2005 May 6;348(3):727-39. PMID:15826667 doi:http://dx.doi.org/10.1016/j.jmb.2005.03.007
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