1hes
MU2 ADAPTIN SUBUNIT (AP50) OF AP2 ADAPTOR (SECOND DOMAIN), COMPLEXED WITH P-SELECTIN INTERNALIZATION PEPTIDE SHLGTYGVFTNAA
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OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Atopy, susceptibility to OMIM:[173610], Platelet alpha/delta storage pool deficiency OMIM:[173610]
About this StructureAbout this Structure
1HES is a Protein complex structure of sequences from Homo sapiens and Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
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
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