2dx5
From Proteopedia
(Difference between revisions)
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<StructureSection load='2dx5' size='340' side='right'caption='[[2dx5]], [[Resolution|resolution]] 3.35Å' scene=''> | <StructureSection load='2dx5' size='340' side='right'caption='[[2dx5]], [[Resolution|resolution]] 3.35Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2dx5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2dx5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DX5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DX5 FirstGlance]. <br> |
| - | </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=2dx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dx5 OCA], [https://pdbe.org/2dx5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dx5 RCSB], [https://www.ebi.ac.uk/pdbsum/2dx5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dx5 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.35Å</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=2dx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dx5 OCA], [https://pdbe.org/2dx5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dx5 RCSB], [https://www.ebi.ac.uk/pdbsum/2dx5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dx5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/VPS36_MOUSE VPS36_MOUSE] Component of the ESCRT-II complex (endosomal sorting complex required for transport II), which is required for multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex. Its ability to bind ubiquitin probably plays a role in endosomal sorting of ubiquitinated cargo proteins by ESCRT complexes. The ESCRT-II complex may also play a role in transcription regulation, possibly via its interaction with ELL. Binds phosphoinosides such as PtdIns(3,4,5)P3 (By similarity). | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=2dx5 ConSurf]. | </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=2dx5 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | ESCRT-II, a complex that sorts ubiquitinated membrane proteins to lysosomes, localizes to endosomes through interaction between the Vps36 subunit's GLUE domain and phosphatidylinositides (PIs). In yeast, a ubiquitin (Ub)-interacting NZF domain is inserted in Vps36 GLUE, whereas its mammalian counterpart, Eap45 GLUE, lacks the NZF domain. In the Eap45 GLUE-Ub complex structure, Ub binds far from the proposed PI-binding site of Eap45 GLUE, suggesting their independent binding. | ||
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| - | Structural basis of ubiquitin recognition by mammalian Eap45 GLUE domain.,Hirano S, Suzuki N, Slagsvold T, Kawasaki M, Trambaiolo D, Kato R, Stenmark H, Wakatsuki S Nat Struct Mol Biol. 2006 Nov;13(11):1031-2. Epub 2006 Oct 22. PMID:17057714<ref>PMID:17057714</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2dx5" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[3D structures of ubiquitin|3D structures of ubiquitin]] | *[[3D structures of ubiquitin|3D structures of ubiquitin]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Mus musculus]] |
| - | [[Category: Hirano | + | [[Category: Hirano S]] |
| - | [[Category: Kato | + | [[Category: Kato R]] |
| - | [[Category: Kawasaki | + | [[Category: Kawasaki M]] |
| - | [[Category: Slagsvold | + | [[Category: Slagsvold T]] |
| - | [[Category: Stenmark | + | [[Category: Stenmark H]] |
| - | [[Category: Suzuki | + | [[Category: Suzuki N]] |
| - | [[Category: Trambaiolo | + | [[Category: Trambaiolo D]] |
| - | [[Category: Wakatsuki | + | [[Category: Wakatsuki S]] |
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Current revision
The complex structure between the mouse EAP45-GLUE domain and ubiquitin
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Categories: Bos taurus | Large Structures | Mus musculus | Hirano S | Kato R | Kawasaki M | Slagsvold T | Stenmark H | Suzuki N | Trambaiolo D | Wakatsuki S
