1GYV: Gamma-adaptin appendage domain from clathrin adaptor AP1, L762E mutant

Citation:
Abstract
The AP1 complex is one of a family of heterotetrameric clathrin-adaptor complexes involved in vesicular trafficking between the Golgi and endosomes. The complex has two large subunits, gamma and beta1, which can be divided into trunk, hinge, and appendage domains. The 1.8 A resolution structure of the gamma appendage is presented. The binding site for the known gamma appendage ligand gamma-synergin is mapped through creation of point mutations designed on the basis of the structure. We also show that Eps15, a protein believed to be involved in vesicle formation at the plasma membrane, is also a ligand of gamma appendage and binds to the same site as gamma-synergin. This observation explains the demonstrated brefeldinA (BFA)-sensitive colocalization of Eps15 and AP1 at the Golgi complex.
PDB ID: 1GYVDownload
MMDB ID: 20344
PDB Deposition Date: 2002/4/30
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 1.71  Å
Source Organism:
Similar Structures:
Biological Unit for 1GYV: monomeric; determined by author and by software (PQS)
Molecular Components in 1GYV
Label Count Molecule
Protein (1 molecule)
1
Adapter-related Protein Complex 1 Gamma 1 Subunit(Gene symbol: Ap1g1)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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