2dwy

From Proteopedia

Revision as of 12:37, 23 January 2008

Crystal Structure Analysis of GGA1-GAE

Overview

Golgi-localizing, gamma-adaptin ear domain homology, ADP ribosylation, factor-binding (GGA) proteins and the adaptor protein (AP) complex, AP-1, are involved in membrane traffic between the trans Golgi network and the, endosomes. The gamma-adaptin ear (GAE) domain of GGAs and the gamma1 ear, domain of AP-1 interact with an acidic phenylalanine motif found in, accessory proteins. The GAE domain of GGA1 (GGA1-GAE) interacts with a, WNSF-containing peptide derived from its own hinge region, although the, peptide sequence deviates from the standard acidic phenylalanine motif. We, report here the structure of GGA1-GAE in complex with the GGA1 hinge, peptide, which revealed that the two aromatic side chains of the WNSF, sequence fit into a hydrophobic groove formed by aliphatic portions of the, side chains of conserved arginine and lysine residues of GGA1-GAE, in a, similar manner to the interaction between GGA-GAEs and acidic, phenylalanine sequences from the accessory proteins. Fluorescence, quenching experiments indicate that the GGA1 hinge region binds to, GGA1-GAE and competes with accessory proteins for binding. Taken together, with the previous observation that gamma1 ear binds to the GGA1 hinge, region, the interaction between the hinge region and the GAE domain, underlies the autoregulation of GGA function in clathrin-mediated, trafficking through competing with the accessory proteins and the AP-1, complex.

About this Structure

2DWY is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Molecular Basis for Autoregulatory Interaction Between GAE Domain and Hinge Region of GGA1., Inoue M, Shiba T, Ihara K, Yamada Y, Hirano S, Kamikubo H, Kataoka M, Kawasaki M, Kato R, Nakayama K, Wakatsuki S, Traffic. 2007 Jul 20;8(7):904-913. Epub 2007 May 16. PMID:17506864

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