2vj0: Difference between revisions

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[[Image:2vj0.jpg|left|200px]]
{{Seed}}
[[Image:2vj0.png|left|200px]]


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{{STRUCTURE_2vj0|  PDB=2vj0  |  SCENE=  }}  
{{STRUCTURE_2vj0|  PDB=2vj0  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF THE ALPHA-ADAPTIN APPENDAGE DOMAIN, FROM THE AP2 ADAPTOR COMPLEX, IN COMPLEX WITH AN FXDNF PEPTIDE FROM AMPHIPHYSIN1 AND A WVXF PEPTIDE FROM SYNAPTOJANIN P170'''
===CRYSTAL STRUCTURE OF THE ALPHA-ADAPTIN APPENDAGE DOMAIN, FROM THE AP2 ADAPTOR COMPLEX, IN COMPLEX WITH AN FXDNF PEPTIDE FROM AMPHIPHYSIN1 AND A WVXF PEPTIDE FROM SYNAPTOJANIN P170===




==Overview==
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Adaptor protein (AP) complexes bind to transmembrane proteins destined for internalization and to membrane lipids, so linking cargo to the accessory internalization machinery. This machinery interacts with the appendage domains of APs, which have platform and beta-sandwich subdomains, forming the binding surfaces for interacting proteins. Proteins that interact with the subdomains do so via short motifs, usually found in regions of low structural complexity of the interacting proteins. So far, up to four motifs have been identified that bind to and partially compete for at least two sites on each of the appendage domains of the AP2 complex. Motifs in individual accessory proteins, their sequential arrangement into motif domains, and partial competition for binding sites on the appendage domains coordinate the formation of endocytic complexes in a temporal and spatial manner. In this work, we examine the dominant interaction sequence in amphiphysin, a synapse-enriched accessory protein, which generates membrane curvature and recruits the scission protein dynamin to the necks of coated pits, for the platform subdomain of the alpha-appendage. The motif domain of amphiphysin1 contains one copy of each of a DX(F/W) and FXDXF motif. We find that the FXDXF motif is the main determinant for the high affinity interaction with the alpha-adaptin appendage. We describe the optimal sequence of the FXDXF motif using thermodynamic and structural data and show how sequence variation controls the affinities of these motifs for the alpha-appendage.
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{{ABSTRACT_PUBMED_17986441}}


==About this Structure==
==About this Structure==
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[[Category: Synaptojanin]]
[[Category: Synaptojanin]]
[[Category: Transport]]
[[Category: Transport]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 18:54:40 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:21:06 2008''

Revision as of 20:21, 28 July 2008

File:2vj0.png

Template:STRUCTURE 2vj0

CRYSTAL STRUCTURE OF THE ALPHA-ADAPTIN APPENDAGE DOMAIN, FROM THE AP2 ADAPTOR COMPLEX, IN COMPLEX WITH AN FXDNF PEPTIDE FROM AMPHIPHYSIN1 AND A WVXF PEPTIDE FROM SYNAPTOJANIN P170

Template:ABSTRACT PUBMED 17986441

About this Structure

2VJ0 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

Solitary and Repetitive Binding Motifs for the AP2 Complex {alpha}-Appendage in Amphiphysin and Other Accessory Proteins., Olesen LE, Ford MG, Schmid EM, Vallis Y, Babu MM, Li PH, Mills IG, McMahon HT, Praefcke GJ, J Biol Chem. 2008 Feb 22;283(8):5099-109. Epub 2007 Nov 6. PMID:17986441

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