1bxx

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Image:1bxx.gif

1bxx, resolution 2.7Å

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

Overview

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.

About this Structure

1BXX is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

A structural explanation for the recognition of tyrosine-based endocytotic signals., Owen DJ, Evans PR, Science. 1998 Nov 13;282(5392):1327-32. PMID:9812899

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