1hes
From Proteopedia
(New page: 200px<br /> <applet load="1hes" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hes, resolution 3.0Å" /> '''MU2 ADAPTIN SUBUNIT ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1hes.gif|left|200px]]<br /> | + | [[Image:1hes.gif|left|200px]]<br /><applet load="1hes" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1hes" size=" | + | |
caption="1hes, resolution 3.0Å" /> | caption="1hes, resolution 3.0Å" /> | ||
'''MU2 ADAPTIN SUBUNIT (AP50) OF AP2 ADAPTOR (SECOND DOMAIN), COMPLEXED WITH P-SELECTIN INTERNALIZATION PEPTIDE SHLGTYGVFTNAA'''<br /> | '''MU2 ADAPTIN SUBUNIT (AP50) OF AP2 ADAPTOR (SECOND DOMAIN), COMPLEXED WITH P-SELECTIN INTERNALIZATION PEPTIDE SHLGTYGVFTNAA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Internalization signals of the Yxx phi type (phi = bulky hydrophobic side | + | 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. |
==Disease== | ==Disease== | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1HES is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http:// | + | 1HES is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HES OCA]. |
==Reference== | ==Reference== | ||
| Line 18: | Line 17: | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
| - | [[Category: Evans, P | + | [[Category: Evans, P R.]] |
| - | [[Category: Green, S | + | [[Category: Green, S A.]] |
| - | [[Category: Owen, D | + | [[Category: Owen, D J.]] |
[[Category: adaptor]] | [[Category: adaptor]] | ||
[[Category: endocytosis]] | [[Category: endocytosis]] | ||
| Line 26: | Line 25: | ||
[[Category: peptide complex]] | [[Category: peptide complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:00:36 2008'' |
Revision as of 11:00, 21 February 2008
|
MU2 ADAPTIN SUBUNIT (AP50) OF AP2 ADAPTOR (SECOND DOMAIN), COMPLEXED WITH P-SELECTIN INTERNALIZATION PEPTIDE SHLGTYGVFTNAA
Contents |
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.
Disease
Known diseases associated with this structure: Atopy, susceptibility to OMIM:[173610], Platelet alpha/delta storage pool deficiency OMIM:[173610]
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 Thu Feb 21 13:00:36 2008
