2bp5: Difference between revisions

Revision as of 02:58, 29 July 2008

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File:2bp5.png

Template:STRUCTURE 2bp5

MU2 ADAPTIN SUBUNIT (AP50) OF AP2 ADAPTOR (SECOND DOMAIN), COMPLEXED WITH NON-CANONICAL INTERNALIZATION PEPTIDE VEDYEQGLSGMU2 ADAPTIN SUBUNIT (AP50) OF AP2 ADAPTOR (SECOND DOMAIN), COMPLEXED WITH NON-CANONICAL INTERNALIZATION PEPTIDE VEDYEQGLSG

Template:ABSTRACT PUBMED 15985462

About this StructureAbout this Structure

2BP5 is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

Non-canonical YXXGPhi endocytic motifs: recognition by AP2 and preferential utilization in P2X4 receptors., Royle SJ, Qureshi OS, Bobanovic LK, Evans PR, Owen DJ, Murrell-Lagnado RD, J Cell Sci. 2005 Jul 15;118(Pt 14):3073-80. Epub 2005 Jun 28. PMID:15985462

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_2bp5|  PDB=2bp5  |  SCENE=  }}
-'''MU2 ADAPTIN SUBUNIT (AP50) OF AP2 ADAPTOR (SECOND DOMAIN), COMPLEXED WITH NON-CANONICAL INTERNALIZATION PEPTIDE VEDYEQGLSG'''
+===MU2 ADAPTIN SUBUNIT (AP50) OF AP2 ADAPTOR (SECOND DOMAIN), COMPLEXED WITH NON-CANONICAL INTERNALIZATION PEPTIDE VEDYEQGLSG===
-==Overview==
+<!--
-During clathrin-mediated endocytosis, proteins on the cell surface are selected for inclusion in clathrin-coated vesicles by clathrin adaptors, mainly the adaptor complex AP2. The P2X4 subtype of ATP-gated ion channel has in its C-terminus two putative endocytic motifs: a canonical YXXPhi motif and a non-canonical YXXGPhi motif (YEQGL). We demonstrate that endocytosis of P2X4 receptors is mediated preferentially by the YXXGPhi motif because the YXXPhi motif is inaccessible to AP2 owing to the structure of the channel. The crystal structure of a complex between residues 160-435 of the mu2 subunit of AP2 and a P2X4 C-terminal peptide showed that the YEQGL motif binds to mu2 at the same site as YXXPhi motifs. Y and Phi residues are accommodated in the same hydrophobic pockets in mu2 with the extra residue between them being accommodated by changes in the peptide's backbone configuration, when compared to YXXPhi motifs. These data demonstrate that the family of potential tyrosine-based endocytic signals must be expanded to include motifs with an additional glycine at Y+3 (YXXGPhi).
+The line below this paragraph, {{ABSTRACT_PUBMED_15985462}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15985462 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15985462}}
 ==About this Structure==
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 [[Category: Endocytosis/exocytosis]]
 [[Category: Peptide complex]]
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