1BXX

MU2 ADAPTIN SUBUNIT (AP50) OF AP2 ADAPTOR (SECOND DOMAIN), COMPLEXED WITH TGN38 INTERNALIZATION PEPTIDE DYQRLN

Summary for 1BXX

• Entry DOI: 10.2210/pdb1bxx/pdb
• Descriptor: PROTEIN (AP50), PROTEIN (TGN38 PEPTIDE) (3 entities in total)
• Functional Keywords: endocytosis, adaptor, peptide complex, endocytosis-exocytosis complex, endocytosis/exocytosis
• Biological source: Rattus norvegicus (Norway rat); More
• Cellular location: Cell membrane : P84092
• Total number of polymer chains: 2
• Total formula weight: 33567.22

Authors

Owen, D.J.,Evans, P.R. (deposition date: 1998-10-08, release date: 1998-11-25, Last modification date: 2023-08-09)

Primary citation

Owen, D.J.,Evans, P.R.
A structural explanation for the recognition of tyrosine-based endocytotic signals.
Science, 282:1327-1332, 1998

PubMed Abstract: Many cell surface proteins are marked for endocytosis by a cytoplasmic sequence motif, tyrosine-X-X-(hydrophobic residue), that is recognized by the mu2 subunit of AP2 adaptors. Crystal structures of the internalization signal binding domain of mu2 complexed with the internalization signal peptides of epidermal growth factor receptor and the trans-Golgi network protein TGN38 have been determined at 2.7 angstrom resolution. The signal peptides adopted an extended conformation rather than the expected tight turn. Specificity was conferred by hydrophobic pockets that bind the tyrosine and leucine in the peptide. In the crystal, the protein forms dimers that could increase the strength and specificity of binding to dimeric receptors.

PubMed: 9812899
DOI: 10.1126/science.282.5392.1327

Experimental method

X-RAY DIFFRACTION (2.7 Å)