2bp5: Difference between revisions

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[[Image:2bp5.gif|left|200px]]<br /><applet load="2bp5" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2bp5.gif|left|200px]]<br /><applet load="2bp5" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2bp5, resolution 2.80Å" />

'''MU2 ADAPTIN SUBUNIT (AP50) OF AP2 ADAPTOR (SECOND DOMAIN), COMPLEXED WITH NON-CANONICAL INTERNALIZATION PEPTIDE VEDYEQGLSG'''<br />

==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).

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).

==About this Structure==

2BP5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2BP5 OCA].

2BP5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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].

==Reference==

Line 13:

[[Category: Protein complex]]

[[Category: Rattus norvegicus]]

[[Category: Evans, P.R.]]

[[Category: Evans, P R.]]

[[Category: Murrell-Lagnado, R.D.]]

[[Category: Murrell-Lagnado, R D.]]

[[Category: Owen, D.J.]]

[[Category: Owen, D J.]]

[[Category: Royle, S.J.]]

[[Category: Royle, S J.]]

[[Category: 3d-structure]]

[[Category: adaptor]]

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[[Category: peptide complex]]

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@@ Line 1: / Line 1: @@
-[[Image:2bp5.gif|left|200px]]<br /><applet load="2bp5" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2bp5.gif|left|200px]]<br /><applet load="2bp5" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2bp5, resolution 2.80&Aring;" />
 '''MU2 ADAPTIN SUBUNIT (AP50) OF AP2 ADAPTOR (SECOND DOMAIN), COMPLEXED WITH NON-CANONICAL INTERNALIZATION PEPTIDE VEDYEQGLSG'''<br />
 ==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).
+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).
 ==About this Structure==
-BP5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BP5 OCA].
+BP5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Protein complex]]
 [[Category: Rattus norvegicus]]
-[[Category: Evans, P.R.]]
+[[Category: Evans, P R.]]
-[[Category: Murrell-Lagnado, R.D.]]
+[[Category: Murrell-Lagnado, R D.]]
-[[Category: Owen, D.J.]]
+[[Category: Owen, D J.]]
-[[Category: Royle, S.J.]]
+[[Category: Royle, S J.]]
 [[Category: 3d-structure]]
 [[Category: adaptor]]
@@ Line 25: / Line 25: @@
 [[Category: peptide complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:51:45 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:40:09 2008''