2c7m: Difference between revisions

Revision as of 12:26, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2c7m.png

Template:STRUCTURE 2c7m

HUMAN RABEX-5 RESIDUES 1-74 IN COMPLEX WITH UBIQUITINHUMAN RABEX-5 RESIDUES 1-74 IN COMPLEX WITH UBIQUITIN

Template:ABSTRACT PUBMED 16499958

About this StructureAbout this Structure

2C7M is a Protein complex structure of sequences from Bos taurus and Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Tue Jul 29 12:26:16 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2c7m.gif|left|200px]]
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 {{STRUCTURE_2c7m|  PDB=2c7m  |  SCENE=  }}
-'''HUMAN RABEX-5 RESIDUES 1-74 IN COMPLEX WITH UBIQUITIN'''
+===HUMAN RABEX-5 RESIDUES 1-74 IN COMPLEX WITH UBIQUITIN===
-==Overview==
+<!--
-The 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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16499958}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16499958 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16499958}}
 ==About this Structure==
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 [[Category: Ubiquitin binding domain]]
 [[Category: Ubl conjugation]]
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