1HES

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

Summary for 1HES

• Entry DOI: 10.2210/pdb1hes/pdb
• Related: 1BW8 1BXX
• Descriptor: CLATHRIN COAT ASSEMBLY PROTEIN AP50, P-SELECTIN PEPTIDE (3 entities in total)
• Functional Keywords: endocytosis/exocytosis, endocytosis, adaptor, peptide complex, peptide binding prote, endocytosis-exocytosis complex
• Biological source: RATTUS NORVEGICUS (NORWAY RAT); More
• Total number of polymer chains: 2
• Total formula weight: 34640.38

Authors

Owen, D.J.,Evans, P.R.,Green, S.A. (deposition date: 2000-11-24, release date: 2001-05-31, Last modification date: 2023-12-13)

Primary citation

Owen, D.J.,Setiadi, H.,Evans, P.R.,Mcever, R.P.,Green, S.A.
A Third Specificity-Determining Site in Mu 2 Adaptin for Sequences Upstream of Yxx Phi Sorting Motifs
Traffic, 2:105-, 2001

PubMed Abstract: 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.

PubMed: 11247301
DOI: 10.1034/J.1600-0854.2001.020205.X

Experimental method

X-RAY DIFFRACTION (3 Å)