2ELA : Crystal Structure of the PTB domain of human APPL1

  • Jiang Li (Contributor)
  • Xuming Mao (Contributor)
  • Lily Q Dong (Contributor)
  • Feng Liu (Contributor)
  • Liang Tong (Contributor)



Experimental Technique/Method:X-RAY DIFFRACTION
Classification:CELL CYCLE
Release Date:2007-05-29
Deposition Date:2007-03-27
Revision Date:2008-04-30#2011-07-13
Molecular Weight:39873.6
Macromolecule Type:Protein
Residue Count:350
Atom Site Count:2182

APPL1 interacts with adiponectin receptors and other important signaling molecules. It contains a BAR and a PH domain near its N terminus, and the two domains may function as a unit (BAR-PH domain). We report here the crystal structures of the BAR-PH and PTB domains of human APPL1. The structures reveal novel features for BAR domain dimerization and for the interactions between the BAR and PH domains. The BAR domain dimer of APPL1 contains two four-helical bundles, whereas other BAR domain dimers have only three helices in each bundle. The PH domain is located at the opposite ends of the BAR domain dimer. Yeast two-hybrid assays confirm the interactions between the BAR and PH domains. Lipid binding assays show that the BAR, PH, and PTB domains can bind phospholipids. The ability of APPL1 to interact with multiple signaling molecules and phospholipids supports an important role for this adaptor in cell signaling.
Datos disponibles2007

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