1GYV
Gamma-adaptin appendage domain from clathrin adaptor AP1, L762E mutant
Summary for 1GYV
| Entry DOI | 10.2210/pdb1gyv/pdb |
| Related | 1GYU 1GYW |
| Descriptor | ADAPTER-RELATED PROTEIN COMPLEX 1 GAMMA 1 SUBUNIT (2 entities in total) |
| Functional Keywords | endocytosis, adaptor, clathrin, golgi, adaptin |
| Biological source | MUS MUSCULUS (MOUSE) |
| Total number of polymer chains | 1 |
| Total formula weight | 13433.23 |
| Authors | Evans, P.R.,Owen, D.J.,McMahon, H.M.,Kent, H.M. (deposition date: 2002-04-30, release date: 2002-08-22, Last modification date: 2023-12-13) |
| Primary citation | Kent, H.M.,McMahon, H.T.,Evans, P.R.,Benmerah, A.,Owen, D.J. Gamma-adaptin appendage domain: structure and binding site for Eps15 and gamma-synergin. Structure, 10:1139-1148, 2002 Cited by PubMed 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. PubMed: 12176391DOI: 10.1016/s0969-2126(02)00801-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.71 Å) |
Structure validation
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