1hes

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[[Image:1hes.gif|left|200px]]
[[Image:1hes.gif|left|200px]]
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{{Structure
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|GENE= AP50 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hes FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hes OCA], [http://www.ebi.ac.uk/pdbsum/1hes PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hes RCSB]</span>
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'''MU2 ADAPTIN SUBUNIT (AP50) OF AP2 ADAPTOR (SECOND DOMAIN), COMPLEXED WITH P-SELECTIN INTERNALIZATION PEPTIDE SHLGTYGVFTNAA'''
'''MU2 ADAPTIN SUBUNIT (AP50) OF AP2 ADAPTOR (SECOND DOMAIN), COMPLEXED WITH P-SELECTIN INTERNALIZATION PEPTIDE SHLGTYGVFTNAA'''
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[[Category: Green, S A.]]
[[Category: Green, S A.]]
[[Category: Owen, D J.]]
[[Category: Owen, D J.]]
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[[Category: adaptor]]
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[[Category: Adaptor]]
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[[Category: endocytosis]]
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[[Category: Endocytosis]]
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[[Category: peptide binding prote]]
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[[Category: Peptide binding prote]]
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[[Category: peptide complex]]
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[[Category: Peptide complex]]
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Revision as of 15:46, 2 May 2008

Template:STRUCTURE 1hes

MU2 ADAPTIN SUBUNIT (AP50) OF AP2 ADAPTOR (SECOND DOMAIN), COMPLEXED WITH P-SELECTIN INTERNALIZATION PEPTIDE SHLGTYGVFTNAA


Overview

Internalization signals of the Yxx phi type (phi = bulky hydrophobic side chain) interact with the mu 2 chain of AP-2 adaptors. Internalization activity is intolerant of non-conservative substitution of either the tyrosine or the phi side chains, which bind to hydrophobic pockets in mu 2 adaptin in a conformation described as 'a two pinned plug into a socket'. P-selectin, a type I transmembrane protein, contains the Yxx phi-like sequence YGVF in its cytoplasmic domain, but substitution of either the tyrosine or phenylalanine with alanine in the full-length protein causes only small changes in the rate of endocytosis. It is shown here that the sequence YGVF contained within a peptide corresponding to the 17 COOH-terminal amino acids of P-selectin binds to mu 2 adaptin in the same fashion previously seen for other Yxx phi motifs. In addition, the P-selectin peptide binds to a third hydrophobic pocket in mu 2 adaptin through a leucine at position Y-3 in the peptide. This structure suggests that some sequences can function as a 'three pinned plug', in which internalization activity is not critically dependent on any one of the three interacting side chains.

About this Structure

1HES is a Protein complex structure of sequences from Homo sapiens and Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

A third specificity-determining site in mu 2 adaptin for sequences upstream of Yxx phi sorting motifs., Owen DJ, Setiadi H, Evans PR, McEver RP, Green SA, Traffic. 2001 Feb;2(2):105-10. PMID:11247301 Page seeded by OCA on Fri May 2 18:46:40 2008

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