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6WCJ

Asymmetric vertex of the clathrin minicoat cage

Summary for 6WCJ
Entry DOI10.2210/pdb6wcj/pdb
EMDB information21608 21609 21610 21611 21612 21613 21614 21615 21616
DescriptorClathrin heavy chain 1, Clathrin light chain B (2 entities in total)
Functional Keywordsclathrin coated vesicle, clathrin heavy chain, clathrin light chain, clathrin cage, endocytosis
Biological sourceBos taurus (Bovine)
More
Total number of polymer chains15
Total formula weight1876859.18
Authors
Paraan, M.,Mendez, J.,Sharum, S.,Kurtin, D.,He, H.,Stagg, S. (deposition date: 2020-03-30, release date: 2020-08-19, Last modification date: 2024-03-06)
Primary citationParaan, M.,Mendez, J.,Sharum, S.,Kurtin, D.,He, H.,Stagg, S.M.
The structures of natively assembled clathrin-coated vesicles.
Sci Adv, 6:eaba8397-eaba8397, 2020
Cited by
PubMed Abstract: Clathrin-coated vesicles mediate trafficking of proteins and nutrients in the cell and between organelles. Proteins included in the clathrin-coated vesicles (CCVs) category include clathrin heavy chain (CHC), clathrin light chain (CLC), and a variety of adaptor protein complexes. Much is known about the structures of the individual CCV components, but data are lacking about the structures of the fully assembled complexes together with membrane and in complex with cargo. Here, we determined the structures of natively assembled CCVs in a variety of geometries. We show that the adaptor β2 appendages crosslink adjacent CHC β-propellers and that the appendage densities are enriched in CCV hexagonal faces. We resolve how adaptor protein 2 and other associated factors in hexagonal faces form an assembly hub with an extensive web of interactions between neighboring β-propellers and propose a structural model that explains how adaptor binding can direct the formation of pentagonal and hexagonal faces.
PubMed: 32743076
DOI: 10.1126/sciadv.aba8397
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (6.3 Å)
Structure validation

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