1HX8
CRYSTAL STRUCTURE OF N-TERMINAL DOMAIN OF DROSOPHILA AP180
Summary for 1HX8
Entry DOI | 10.2210/pdb1hx8/pdb |
Related | 1dvp |
Descriptor | SYNAPSE-ENRICHED CLATHRIN ADAPTOR PROTEIN LAP, SULFATE ION (3 entities in total) |
Functional Keywords | all alpha, alpha helices repeats, coiled-coil, endocytosis-exocytosis complex, endocytosis/exocytosis |
Biological source | Drosophila melanogaster (fruit fly) |
Total number of polymer chains | 2 |
Total formula weight | 67487.95 |
Authors | Mao, Y.,Chen, J.,Maynard, J.A.,Zhang, B.,Quiocho, F.A. (deposition date: 2001-01-12, release date: 2001-02-28, Last modification date: 2024-02-07) |
Primary citation | Mao, Y.,Chen, J.,Maynard, J.A.,Zhang, B.,Quiocho, F.A. A novel all helix fold of the AP180 amino-terminal domain for phosphoinositide binding and clathrin assembly in synaptic vesicle endocytosis. Cell(Cambridge,Mass.), 104:433-440, 2001 Cited by PubMed Abstract: Clathrin-mediated endocytosis plays a major role in retrieving synaptic vesicles from the plasma membrane following exocytosis. This endocytic process requires AP180 (or a homolog), which promotes the assembly and restricts the size of clathrin-coated vesicles. The highly conserved 33 kDa amino-terminal domain of AP180 plays a critical role in binding to phosphoinositides and in regulating the clathrin assembly activity of AP180. The crystal structure of the amino-terminal domain reported herein reveals a novel fold consisting of a large double layer of sheets of ten alpha helices and a unique site for binding phosphoinositides. The finding that the clathrin-box motif is mostly buried and lies in a helix indicates a different site and mechanism for binding of the domain to clathrins than previously assumed. PubMed: 11239400DOI: 10.1016/S0092-8674(01)00230-6 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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