1E42

Beta2-adaptin appendage domain, from clathrin adaptor AP2

Summary for 1E42

• Entry DOI: 10.2210/pdb1e42/pdb
• Descriptor: AP-2 COMPLEX SUBUNIT BETA, DITHIANE DIOL, MAGNESIUM ION, ... (7 entities in total)
• Functional Keywords: endocytosis, adaptor
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cell membrane: P63010
• Total number of polymer chains: 2
• Total formula weight: 58963.29

Authors

Owen, D.J.,Evans, P.R.,McMahon, H.T. (deposition date: 2000-06-27, release date: 2000-08-21, Last modification date: 2024-05-08)

Primary citation

Owen, D.J.,Vallis, Y.,Pearse, B.M.F.,Mcmahon, H.T.,Evans, P.R.
The Structure and Function of the Beta2-Adaptin Appendage Domain
Embo J., 19:4216-, 2000

PubMed Abstract: The heterotetrameric AP2 adaptor (alpha, beta 2, mu 2 and sigma 2 subunits) plays a central role in clathrin-mediated endocytosis. We present the protein recruitment function and 1.7 A resolution structure of its beta 2-appendage domain to complement those previously determined for the mu 2 subunit and alpha appendage. Using structure-directed mutagenesis, we demonstrate the ability of the beta 2 appendage alone to bind directly to clathrin and the accessory proteins AP180, epsin and eps15 at the same site. Clathrin polymerization is promoted by binding of clathrin simultaneously to the beta 2-appendage site and to a second site on the adjacent beta 2 hinge. This results in the displacement of the other ligands from the beta 2 appendage. Thus clathrin binding to an AP2-accessory protein complex would cause the controlled release of accessory proteins at sites of vesicle formation.

PubMed: 10944104
DOI: 10.1093/EMBOJ/19.16.4216

Experimental method

X-RAY DIFFRACTION (1.7 Å)