1B9K

ALPHA-ADAPTIN APPENDAGE DOMAIN, FROM CLATHRIN ADAPTOR AP2

Summary for 1B9K

• Entry DOI: 10.2210/pdb1b9k/pdb
• Descriptor: PROTEIN (ALPHA-ADAPTIN APPENDAGE DOMAIN) (2 entities in total)
• Functional Keywords: endocytosis, adaptor, endocytosis-exocytosis complex, endocytosis/exocytosis
• Biological source: Mus musculus (house mouse)
• Cellular location: Cell membrane: P17427
• Total number of polymer chains: 1
• Total formula weight: 27016.77

Authors

Owen, D.J.,Evans, P.R. (deposition date: 1999-02-11, release date: 1999-07-06, Last modification date: 2023-12-27)

Primary citation

Owen, D.J.,Vallis, Y.,Noble, M.E.,Hunter, J.B.,Dafforn, T.R.,Evans, P.R.,McMahon, H.T.
A structural explanation for the binding of multiple ligands by the alpha-adaptin appendage domain.
Cell(Cambridge,Mass.), 97:805-815, 1999

PubMed Abstract: The alpha subunit of the endocytotic AP2 adaptor complex contains a 30 kDa "appendage" domain, which is joined to the rest of the protein via a flexible linker. The 1.9 A resolution crystal structure of this domain reveals a single binding site for its ligands, which include amphiphysin, Eps15, and epsin. This domain when overexpressed in COS7 fibroblasts is shown to inhibit transferrin uptake, whereas mutants in which interactions with its binding partners are abolished do not. DPF/W motifs present in appendage domain-binding partners are shown to play a crucial role in their interactions with the domain. A single site for binding multiple ligands would allow for temporal and spatial regulation in the recruitment of components of the endocytic machinery.

PubMed: 10380931
DOI: 10.1016/S0092-8674(00)80791-6

Experimental method

X-RAY DIFFRACTION (1.9 Å)