PDBsum entry 3l81

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Transport protein PDB id
Protein chain
250 a.a. *
GOL ×3
Waters ×153
* Residue conservation analysis
PDB id:
Name: Transport protein
Title: Crystal structure of adaptor protein complex 4 (ap-4) mu4 su terminal domain, in complex with a sorting peptide from the precursor protein (app)
Structure: Ap-4 complex subunit mu-1. Chain: a. Fragment: c-terminus, residues 160-453. Synonym: adapter-related protein complex 4 mu-1 subunit, ap complex mu subunit, mu subunit of ap-4, mu4-adaptin, mu4, m related protein 2, mu-arp2. Engineered: yes. Mutation: yes. Amyloid beta a4 protein.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ap4m1, muarp2. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes
1.60Å     R-factor:   0.209     R-free:   0.252
Authors: G.A.Mardones,A.L.Rojas,P.V.Burgos,L.L.P.Dasilva,Y.Prabhu, J.S.Bonifacino,J.H.Hurley
Key ref: P.V.Burgos et al. (2010). Sorting of the Alzheimer's disease amyloid precursor protein mediated by the AP-4 complex. Dev Cell, 18, 425-436. PubMed id: 20230749
29-Dec-09     Release date:   02-Jun-10    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
O00189  (AP4M1_HUMAN) -  AP-4 complex subunit mu-1
453 a.a.
250 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     clathrin adaptor complex   1 term 
  Biological process     vesicle-mediated transport   2 terms 


Dev Cell 18:425-436 (2010)
PubMed id: 20230749  
Sorting of the Alzheimer's disease amyloid precursor protein mediated by the AP-4 complex.
P.V.Burgos, G.A.Mardones, A.L.Rojas, L.L.daSilva, Y.Prabhu, J.H.Hurley, J.S.Bonifacino.
Adaptor protein 4 (AP-4) is the most recently discovered and least well-characterized member of the family of heterotetrameric adaptor protein (AP) complexes that mediate sorting of transmembrane cargo in post-Golgi compartments. Herein, we report the interaction of an YKFFE sequence from the cytosolic tail of the Alzheimer's disease amyloid precursor protein (APP) with the mu4 subunit of AP-4. Biochemical and X-ray crystallographic analyses reveal that the properties of the APP sequence and the location of the binding site on mu4 are distinct from those of other signal-adaptor interactions. Disruption of the APP-AP-4 interaction decreases localization of APP to endosomes and enhances gamma-secretase-catalyzed cleavage of APP to the pathogenic amyloid-beta peptide. These findings demonstrate that APP and AP-4 engage in a distinct type of signal-adaptor interaction that mediates transport of APP from the trans-Golgi network (TGN) to endosomes, thereby reducing amyloidogenic processing of the protein.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20685960 F.J.Pérez-Victoria, C.Schindler, J.G.Magadán, G.A.Mardones, C.Delevoye, M.Romao, G.Raposo, and J.S.Bonifacino (2010).
Ang2/fat-free is a conserved subunit of the Golgi-associated retrograde protein complex.
  Mol Biol Cell, 21, 3386-3395.  
  21054155 M.Anitei, T.Wassmer, C.Stange, and B.Hoflack (2010).
Bidirectional transport between the trans-Golgi network and the endosomal system.
  Mol Membr Biol, 27, 443-456.  
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