2c7m: Difference between revisions
No edit summary |
No edit summary |
||
Line 3: | Line 3: | ||
<StructureSection load='2c7m' size='340' side='right'caption='[[2c7m]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='2c7m' size='340' side='right'caption='[[2c7m]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2c7m]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2c7m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C7M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C7M FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><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> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1aar|1aar]], [[1e0q|1e0q]], [[1p3q|1p3q]], [[1uzx|1uzx]], [[1v80|1v80]], [[1v81|1v81]], [[1wr6|1wr6]], [[1wrd|1wrd]], [[1yd8|1yd8]], [[2bgf|2bgf]], [[2c7n|2c7n]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1aar|1aar]], [[1e0q|1e0q]], [[1p3q|1p3q]], [[1uzx|1uzx]], [[1v80|1v80]], [[1v81|1v81]], [[1wr6|1wr6]], [[1wrd|1wrd]], [[1yd8|1yd8]], [[2bgf|2bgf]], [[2c7n|2c7n]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2c7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c7m OCA], [https://pdbe.org/2c7m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c7m RCSB], [https://www.ebi.ac.uk/pdbsum/2c7m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c7m ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/RABX5_HUMAN RABX5_HUMAN]] Rab effector protein acting as linker between gamma-adaptin, RAB4A or RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Stimulates nucleotide exchange on RAB5A. Can act as a ubiquitin ligase (By similarity).<ref>PMID:9323142</ref> <ref>PMID:11452015</ref> <ref>PMID:15339665</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Line 32: | Line 32: | ||
==See Also== | ==See Also== | ||
*[[Rab5 GDP/GTP exchange factor|Rab5 GDP/GTP exchange factor]] | *[[Rab5 GDP/GTP exchange factor|Rab5 GDP/GTP exchange factor]] | ||
*[[ | *[[3D structures of ubiquitin|3D structures of ubiquitin]] | ||
== References == | == References == | ||
<references/> | <references/> |
Revision as of 13:33, 17 February 2021
Human Rabex-5 residues 1-74 in complex with UbiquitinHuman Rabex-5 residues 1-74 in complex with Ubiquitin
Structural highlights
Function[RABX5_HUMAN] Rab effector protein acting as linker between gamma-adaptin, RAB4A or RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Stimulates nucleotide exchange on RAB5A. Can act as a ubiquitin ligase (By similarity).[1] [2] [3] 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 PubMedThe interaction between ubiquitinated proteins and intracellular proteins harboring ubiquitin binding domains (UBDs) is critical to a multitude of cellular processes. Here, we report that Rabex-5, a guanine nucleotide exchange factor for Rab5, binds to Ub through two independent UBDs. These UBDs determine a number of properties of Rabex-5, including its coupled monoubiquitination and interaction in vivo with ubiquitinated EGFRs. Structural and biochemical characterization of the UBDs of Rabex-5 revealed that one of them (MIU, motif interacting with ubiquitin) binds to Ub with modes superimposable to those of the UIM (ubiquitin-interacting motif):Ub interaction, although in the opposite orientation. The other UBD, RUZ (Rabex-5 ubiquitin binding zinc finger) binds to a surface of Ub centered on Asp58(Ub) and distinct from the "canonical" Ile44(Ub)-based surface. The two binding surfaces allow Ub to interact simultaneously with different UBDs, thus opening new perspectives in Ub-mediated signaling. Crystal structure of the ubiquitin binding domains of rabex-5 reveals two modes of interaction with ubiquitin.,Penengo L, Mapelli M, Murachelli AG, Confalonieri S, Magri L, Musacchio A, Di Fiore PP, Polo S, Schneider TR Cell. 2006 Mar 24;124(6):1183-95. Epub 2006 Feb 23. PMID:16499958[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
|