2g30
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beta appendage of AP2 complexed with ARH peptide
OverviewOverview
Clathrin-associated sorting proteins (CLASPs) expand the repertoire of, endocytic cargo sorted into clathrin-coated vesicles beyond the, transmembrane proteins that bind physically to the AP-2 adaptor. LDL and, GPCRs are internalized by ARH and beta-arrestin, respectively. We show, that these two CLASPs bind selectively to the AP-2 beta2 appendage, platform via an alpha-helical [DE](n)X(1-2)FXX[FL]XXXR motif, and that, this motif also occurs and is functional in the epsins. In beta-arrestin, this motif maintains the endocytosis-incompetent state by binding back on, the folded core of the protein in a beta strand conformation. Triggered, via a beta-arrestin/GPCR interaction, the motif must be displaced and must, undergo a strand to helix transition to enable the beta2 appendage binding, that drives GPCR-beta-arrestin complexes into clathrin coats. Another, interaction surface on the beta2 appendage sandwich is identified for, proteins such as eps15 and clathrin, suggesting a mechanism by which, clathrin displaces eps15 to lattice edges during assembly.
DiseaseDisease
Known diseases associated with this structure: Hypercholesterolemia, familial, autosomal recessive OMIM:[605747]
About this StructureAbout this Structure
2G30 is a Protein complex structure of sequences from Homo sapiens. The following page contains interesting information on the relation of 2G30 with [Clathrin]. Full crystallographic information is available from OCA.
ReferenceReference
Molecular switches involving the AP-2 beta2 appendage regulate endocytic cargo selection and clathrin coat assembly., Edeling MA, Mishra SK, Keyel PA, Steinhauser AL, Collins BM, Roth R, Heuser JE, Owen DJ, Traub LM, Dev Cell. 2006 Mar;10(3):329-42. PMID:16516836
Page seeded by OCA on Mon Nov 12 22:13:55 2007