1QTP

CRYSTAL STRUCTURE OF THE AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE

Summary for 1QTP

• Entry DOI: 10.2210/pdb1qtp/pdb
• Descriptor: AP-2 CLATHRIN ADAPTOR ALPHA SUBUNIT (ALPHA-ADAPTIN C) (2 entities in total)
• Functional Keywords: four-wavelength mad, selenomethionine, membrane protein
• Biological source: Mus musculus (house mouse)
• Cellular location: Cell membrane: P17427
• Total number of polymer chains: 1
• Total formula weight: 28016.25

Authors

Traub, L.M.,Downs, M.A.,Westrich, J.L.,Fremont, D.H. (deposition date: 1999-06-28, release date: 1999-07-12, Last modification date: 2024-11-20)

Primary citation

Traub, L.M.,Downs, M.A.,Westrich, J.L.,Fremont, D.H.
Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly.
Proc.Natl.Acad.Sci.USA, 96:8907-8912, 1999

PubMed Abstract: AP-2 adaptors regulate clathrin-bud formation at the cell surface by recruiting clathrin trimers to the plasma membrane and by selecting certain membrane proteins for inclusion within the developing clathrin-coat structure. These functions are performed by discrete subunits of the adaptor heterotetramer. The carboxyl-terminal appendage of the AP-2 alpha subunit appears to regulate the translocation of several endocytic accessory proteins to the bud site. We have determined the crystal structure of the alpha appendage at 1.4-A resolution by multiwavelength anomalous diffraction phasing. It is composed of two distinct structural modules, a beta-sandwich domain and a mixed alpha-beta platform domain. Structure-based mutagenesis shows that alterations to the molecular surface of a highly conserved region on the platform domain differentially affect associations of the appendage with amphiphysin, eps15, epsin, and AP180, revealing a common protein-binding interface.

PubMed: 10430869
DOI: 10.1073/pnas.96.16.8907

Experimental method

X-RAY DIFFRACTION (1.6 Å)