2c7n: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2c7n]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C7N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C7N FirstGlance]. <br> | <table><tr><td colspan='2'>[[2c7n]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C7N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C7N FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>< | </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> | ||
<tr><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]], [[2c7m|2c7m]]</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]], [[2c7m|2c7m]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c7n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2c7n RCSB], [http://www.ebi.ac.uk/pdbsum/2c7n PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c7n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2c7n RCSB], [http://www.ebi.ac.uk/pdbsum/2c7n PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== 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: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Confalioneri, S | [[Category: Confalioneri, S]] | ||
[[Category: Fiore, P P.Di | [[Category: Fiore, P P.Di]] | ||
[[Category: Magri, L | [[Category: Magri, L]] | ||
[[Category: Mapelli, M | [[Category: Mapelli, M]] | ||
[[Category: Murachelli, A G | [[Category: Murachelli, A G]] | ||
[[Category: Musacchio, A | [[Category: Musacchio, A]] | ||
[[Category: Penengo, L | [[Category: Penengo, L]] | ||
[[Category: Polo, S | [[Category: Polo, S]] | ||
[[Category: Schneider, T R | [[Category: Schneider, T R]] | ||
[[Category: Endocytosis]] | [[Category: Endocytosis]] | ||
[[Category: Nuclear protein]] | [[Category: Nuclear protein]] | ||
Revision as of 16:28, 25 December 2014
HUMAN RABEX-5 RESIDUES 1-74 IN COMPLEX WITH UBIQUITINHUMAN RABEX-5 RESIDUES 1-74 IN COMPLEX WITH UBIQUITIN
Structural highlights
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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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