2vj0

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Revision as of 09:28, 23 January 2008

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spinqualitylabelsall models 2vj0, resolution 1.600Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Adaptor protein (AP) complexes bind to transmembrane proteins destined for, internalisation and to membrane lipids, so linking cargo to the accessory, internalisation 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 which 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 which 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 DxF/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.

About this Structure

2VJ0 is a Protein complex structure of sequences from Mus musculus with , , and as ligands. Known structural/functional Sites: , , , , and . 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 P, Mills IG, McMahon HT, Praefcke GJ, J Biol Chem. 2007 Nov 6;. PMID:17986441

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