Publication Date:
1998-11-13
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Owen, D J -- Evans, P R -- New York, N.Y. -- Science. 1998 Nov 13;282(5392):1327-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9812899" target="_blank"〉PubMed〈/a〉
Keywords:
*Adaptor Protein Complex 1
;
Adaptor Protein Complex 2
;
*Adaptor Protein Complex 3
;
Adaptor Protein Complex alpha Subunits
;
*Adaptor Protein Complex mu Subunits
;
Adaptor Proteins, Vesicular Transport
;
Amino Acid Sequence
;
Animals
;
Binding Sites
;
Crystallography, X-Ray
;
Dimerization
;
*Endocytosis
;
*Glycoproteins
;
Humans
;
Hydrogen Bonding
;
Membrane Glycoproteins/*chemistry/metabolism
;
Membrane Proteins/*chemistry/metabolism
;
Models, Molecular
;
Molecular Sequence Data
;
Phosphorylation
;
Protein Conformation
;
Protein Sorting Signals/*chemistry/metabolism
;
Protein Structure, Secondary
;
Receptor, Epidermal Growth Factor/*chemistry/metabolism
;
Tyrosine/chemistry/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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