1wr6: Difference between revisions

Revision as of 04:45, 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:1wr6.png

Template:STRUCTURE 1wr6

Crystal structure of GGA3 GAT domain in complex with ubiquitinCrystal structure of GGA3 GAT domain in complex with ubiquitin

Template:ABSTRACT PUBMED 15966896

About this StructureAbout this Structure

1WR6 is a Protein complex structure of sequences from Bos taurus and Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Molecular mechanism of ubiquitin recognition by GGA3 GAT domain., Kawasaki M, Shiba T, Shiba Y, Yamaguchi Y, Matsugaki N, Igarashi N, Suzuki M, Kato R, Kato K, Nakayama K, Wakatsuki S, Genes Cells. 2005 Jul;10(7):639-54. PMID:15966896

Page seeded by OCA on Tue Jul 29 04:45:10 2008

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OCA

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-'''Crystal structure of GGA3 GAT domain in complex with ubiquitin'''
+===Crystal structure of GGA3 GAT domain in complex with ubiquitin===
-==Overview==
+<!--
-GGA (Golgi-localizing, gamma-adaptin ear domain homology, ARF-binding) proteins, which constitute a family of clathrin coat adaptor proteins, have recently been shown to be involved in the ubiquitin-dependent sorting of receptors, through the interaction between the C-terminal three-helix-bundle of the GAT (GGA and Tom1) domain (C-GAT) and ubiquitin. We report here the crystal structure of human GGA3 C-GAT in complex with ubiquitin. A hydrophobic patch on C-GAT helices alpha1 and alpha2 forms a binding site for the hydrophobic Ile44 surface of ubiquitin. Two distinct orientations of ubiquitin Arg42 determine the shape and the charge distribution of ubiquitin Ile44 surface, leading to two different binding modes. Biochemical and NMR data strongly suggest another hydrophobic binding site on C-GAT helices alpha2 and alpha3, opposite to the first binding site, also binds ubiquitin although weakly. The double-sided ubiquitin binding provides the GAT domain with higher efficiency in recognizing ubiquitinated receptors for lysosomal receptor degradation.
+The line below this paragraph, {{ABSTRACT_PUBMED_15966896}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15966896 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15966896}}
 ==About this Structure==
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 [[Category: Three-helix bundle]]
 [[Category: Ubiquitin-binding protein]]
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