View source for 1kyd

[[Image:1kyd.gif|left|200px]]

 {{Structure
|PDB= 1kyd |SIZE=350|CAPTION= <scene name='initialview01'>1kyd</scene>, resolution 2.00&Aring;
|SITE= 
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
|ACTIVITY= 
|GENE= 
}}

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


==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.

==About this Structure==
1KYD is a [[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=1KYD OCA]. 

==Reference==
Accessory protein recruitment motifs in clathrin-mediated endocytosis., Brett TJ, Traub LM, Fremont DH, Structure. 2002 Jun;10(6):797-809. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12057195 12057195]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Brett, T J.]]
[[Category: Fremont, D H.]]
[[Category: Traub, L M.]]
[[Category: SO4]]
[[Category: endocytosis]]
[[Category: protein-peptide complex]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:23:51 2008''