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New page: left|200px<br /><applet load="1kyf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kyf, resolution 1.22Å" /> '''AP-2 CLATHRIN ADAPTO...
 
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[[Image:1kyf.gif|left|200px]]<br /><applet load="1kyf" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1kyf.gif|left|200px]]<br /><applet load="1kyf" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1kyf, resolution 1.22&Aring;" />
caption="1kyf, resolution 1.22&Aring;" />
'''AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH EPS15 DPF PEPTIDE'''<br />
'''AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH EPS15 DPF PEPTIDE'''<br />


==Overview==
==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==
==About this Structure==
1KYF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KYF OCA].  
1KYF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KYF OCA].  


==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[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: endocytosis]]
[[Category: endocytosis]]
[[Category: protein-peptide complex]]
[[Category: protein-peptide complex]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:04:00 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:39:17 2008''