This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1bw8
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1bw8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bw8, resolution 2.65Å" /> '''MU2 ADAPTIN SUBUNIT ...)
Next diff →
Revision as of 09:50, 20 November 2007
|
MU2 ADAPTIN SUBUNIT (AP50) OF AP2 ADAPTOR (SECOND DOMAIN), COMPLEXED WITH EGFR INTERNALIZATION PEPTIDE FYRALM
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
1BW8 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
Page seeded by OCA on Tue Nov 20 11:58:09 2007
