2bp5: Difference between revisions
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[[Image: | ==MU2 ADAPTIN SUBUNIT (AP50) OF AP2 ADAPTOR (SECOND DOMAIN), COMPLEXED WITH NON-CANONICAL INTERNALIZATION PEPTIDE VEDYEQGLSG== | ||
<StructureSection load='2bp5' size='340' side='right' caption='[[2bp5]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2bp5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BP5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BP5 FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bw8|1bw8]], [[1bxx|1bxx]], [[1gw5|1gw5]], [[1hes|1hes]], [[1i31|1i31]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bp5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bp5 RCSB], [http://www.ebi.ac.uk/pdbsum/2bp5 PDBsum]</span></td></tr> | |||
<table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bp/2bp5_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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). | |||
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<ref>PMID:15985462</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | |||
*[[Adaptin|Adaptin]] | |||
== | == References == | ||
[[ | <references/> | ||
__TOC__ | |||
== | </StructureSection> | ||
< | |||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Evans, P R.]] | [[Category: Evans, P R.]] | ||
Revision as of 05:19, 30 September 2014
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
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedDuring 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). 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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