2ELB
Crystal Structure of the BAR-PH domain of human APPL1
Summary for 2ELB
| Entry DOI | 10.2210/pdb2elb/pdb |
| Related | 2ELA |
| Descriptor | Adapter protein containing PH domain, PTB domain and leucine zipper motif 1 (1 entity in total) |
| Functional Keywords | appl, bar domain, ph domain, protein binding |
| Biological source | Homo sapiens (human) |
| Cellular location | Early endosome membrane; Peripheral membrane protein: Q9UKG1 |
| Total number of polymer chains | 1 |
| Total formula weight | 45987.12 |
| Authors | Li, J.,Mao, X.,Dong, L.Q.,Liu, F.,Tong, L. (deposition date: 2007-03-27, release date: 2007-05-29, Last modification date: 2024-11-06) |
| Primary citation | Li, J.,Mao, X.,Dong, L.Q.,Liu, F.,Tong, L. Crystal Structures of the BAR-PH and PTB Domains of Human APPL1 Structure, 15:525-533, 2007 Cited by PubMed Abstract: 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. PubMed: 17502098DOI: 10.1016/j.str.2007.03.011 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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