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Cited by 583

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

A Structural Explanation for the Recognition of Tyrosine-Based Endocytotic Signals

Open access
Owen, David J., Evans, Philip R.·1998·Science

Abstract

Many cell surface proteins are marked for endocytosis by a cytoplasmic sequence motif, tyrosine-X-X-(hydrophobic residue), that is recognized by the μ2 subunit of AP2 adaptors. Crystal structures of the internalization signal binding domain of μ2 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.

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Crossref · 10.1126/science.282.5392.1327

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Metadata

Authors
Owen, D. J., & Evans, P. R.
Venue
Science
Published
1998-11-13
Volume
282
Issue
5392
Pages
1327-1332
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W1987672004
Cited by
583
References
1
FWCI
12.05
Type
journal article
Language
en
Open access
green

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