1kyd: Difference between revisions

Revision as of 14:39, 21 February 2008

AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH EPSIN DPW PEPTIDE

OverviewOverview

Clathrin-mediated endocytosis depends upon the interaction of accessory proteins with the alpha-ear of the AP-2 adaptor. We present structural characterization of these regulatory interactions. DPF and DPW motif peptides derived from eps15 and epsin bind in type I beta turn conformations to a conserved pocket on the alpha-ear platform. We show evidence for a second binding site that is DPW motif specific. The structure of a complex with an AP-2 binding segment from amphiphysin reveals a novel binding motif that we term FxDxF, which is engaged in an extended conformation by a unique surface of the platform domain. The FxDxF motif is also used by AP180 and the 170 kDa isoform of synaptojanin and can be found in several potential endocytic proteins, including HIP1, CD2AP, and PLAP. A mechanism of clathrin assembly regulation is suggested by three different AP-2 engagement modes.

About this StructureAbout this Structure

1KYD is a Protein complex structure of sequences from Mus musculus with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Accessory protein recruitment motifs in clathrin-mediated endocytosis., Brett TJ, Traub LM, Fremont DH, Structure. 2002 Jun;10(6):797-809. PMID:12057195

Page seeded by OCA on Thu Feb 21 13:39:20 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1kyd.gif|left|200px]]<br />
+[[Image:1kyd.gif|left|200px]]<br /><applet load="1kyd" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1kyd" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1kyd, resolution 2.00&Aring;" />
 '''AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH EPSIN DPW PEPTIDE'''<br />
 ==Overview==
-Clathrin-mediated endocytosis depends upon the interaction of accessory, proteins with the alpha-ear of the AP-2 adaptor. We present structural, characterization of these regulatory interactions. DPF and DPW motif, peptides derived from eps15 and epsin bind in type I beta turn, conformations to a conserved pocket on the alpha-ear platform. We show, evidence for a second binding site that is DPW motif specific. The, structure of a complex with an AP-2 binding segment from amphiphysin, reveals a novel binding motif that we term FxDxF, which is engaged in an, extended conformation by a unique surface of the platform domain. The, FxDxF motif is also used by AP180 and the 170 kDa isoform of synaptojanin, and can be found in several potential endocytic proteins, including HIP1, CD2AP, and PLAP. A mechanism of clathrin assembly regulation is suggested, by three different AP-2 engagement modes.
+Clathrin-mediated endocytosis depends upon the interaction of accessory proteins with the alpha-ear of the AP-2 adaptor. We present structural characterization of these regulatory interactions. DPF and DPW motif peptides derived from eps15 and epsin bind in type I beta turn conformations to a conserved pocket on the alpha-ear platform. We show evidence for a second binding site that is DPW motif specific. The structure of a complex with an AP-2 binding segment from amphiphysin reveals a novel binding motif that we term FxDxF, which is engaged in an extended conformation by a unique surface of the platform domain. The FxDxF motif is also used by AP180 and the 170 kDa isoform of synaptojanin and can be found in several potential endocytic proteins, including HIP1, CD2AP, and PLAP. A mechanism of clathrin assembly regulation is suggested by three different AP-2 engagement modes.
 ==About this Structure==
-KYD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KYD OCA].
+KYD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KYD OCA].
 ==Reference==
@@ Line 14: / Line 13: @@
 [[Category: Mus musculus]]
 [[Category: Protein complex]]
-[[Category: Brett, T.J.]]
+[[Category: Brett, T J.]]
-[[Category: Fremont, D.H.]]
+[[Category: Fremont, D H.]]
-[[Category: Traub, L.M.]]
+[[Category: Traub, L M.]]
 [[Category: SO4]]
 [[Category: endocytosis]]
 [[Category: protein-peptide complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:55:53 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:39:20 2008''