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1HX8

CRYSTAL STRUCTURE OF N-TERMINAL DOMAIN OF DROSOPHILA AP180

Summary for 1HX8
Entry DOI10.2210/pdb1hx8/pdb
Related1dvp
DescriptorSYNAPSE-ENRICHED CLATHRIN ADAPTOR PROTEIN LAP, SULFATE ION (3 entities in total)
Functional Keywordsall alpha, alpha helices repeats, coiled-coil, endocytosis-exocytosis complex, endocytosis/exocytosis
Biological sourceDrosophila melanogaster (fruit fly)
Total number of polymer chains2
Total formula weight67487.95
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 citationMao, 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: 11239400
DOI: 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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数据于2025-08-06公开中

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