1hes: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:1hes.gif|left|200px]]
{{Seed}}
[[Image:1hes.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1hes|  PDB=1hes  |  SCENE=  }}  
{{STRUCTURE_1hes|  PDB=1hes  |  SCENE=  }}  


'''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===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_11247301}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 11247301 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_11247301}}


==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Peptide binding prote]]
[[Category: Peptide binding prote]]
[[Category: Peptide complex]]
[[Category: Peptide complex]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:46:40 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:05:24 2008''

Revision as of 05:05, 1 July 2008

File:1hes.png

Template:STRUCTURE 1hes

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

Template:ABSTRACT PUBMED 11247301

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 Tue Jul 1 08:05:24 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1hes&oldid=606816"