1W80

Crystal structure of the alpha-adaptin appendage domain, from the AP2 adaptor complex, bound to 2 peptides from Synaptojanin170

Summary for 1W80

• Entry DOI: 10.2210/pdb1w80/pdb
• Related: 1B9K 1GW5 1KY6 1KY7 1KYD 1KYF 1KYU 1QTP 1QTS
• Descriptor: ADAPTER-RELATED PROTEIN COMPLEX 2 ALPHA 2 SUBUNIT, SYNAPTOJANIN 1, BENZAMIDINE, ... (8 entities in total)
• Functional Keywords: endocytosis/exocytosis, endocytosis, alpha-adaptin appendage, adaptor complex, ap2, synaptojanin, exocytosis, lipid-binding, endocytosis-exocytosis complex
• Biological source: MUS MUSCULUS (MOUSE); More
• Cellular location: Cell membrane: P17427; Cytoplasm (By similarity): O43426 O43426
• Total number of polymer chains: 3
• Total formula weight: 31404.42

Authors

Ford, M.G.J.,Praefcke, G.J.K.,McMahon, H.T. (deposition date: 2004-09-14, release date: 2004-10-27, Last modification date: 2023-12-13)

Primary citation

Praefcke, G.J.K.,Ford, M.G.J.,Schmid, E.M.,Olesen, L.E.,Gallop, J.L.,Peak-Chew, S.-Y.,Vallis, Y.,Babu, M.M.,Mills, I.G.,Mcmahon, H.T.
Evolving Nature of the Ap2 Alpha-Appendage Hub During Clathrin-Coated Vesicle Endocytosis.
Embo J., 23:4371-, 2004

PubMed Abstract: Clathrin-mediated endocytosis involves the assembly of a network of proteins that select cargo, modify membrane shape and drive invagination, vesicle scission and uncoating. This network is initially assembled around adaptor protein (AP) appendage domains, which are protein interaction hubs. Using crystallography, we show that FxDxF and WVxF peptide motifs from synaptojanin bind to distinct subdomains on alpha-appendages, called 'top' and 'side' sites. Appendages use both these sites to interact with their binding partners in vitro and in vivo. Occupation of both sites simultaneously results in high-affinity reversible interactions with lone appendages (e.g. eps15 and epsin1). Proteins with multiple copies of only one type of motif bind multiple appendages and so will aid adaptor clustering. These clustered alpha(appendage)-hubs have altered properties where they can sample many different binding partners, which in turn can interact with each other and indirectly with clathrin. In the final coated vesicle, most appendage binding partners are absent and thus the functional status of the appendage domain as an interaction hub is temporal and transitory giving directionality to vesicle assembly.

PubMed: 15496985
DOI: 10.1038/SJ.EMBOJ.7600445

Experimental method

X-RAY DIFFRACTION (1.9 Å)