2elb
From Proteopedia
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==Overview== | ==Overview== | ||
| - | APPL1 interacts with adiponectin receptors and other important signaling | + | 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. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Crystal | + | Crystal structures of the BAR-PH and PTB domains of human APPL1., Li J, Mao X, Dong LQ, Liu F, Tong L, Structure. 2007 May;15(5):525-33. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17502098 17502098] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Dong, L | + | [[Category: Dong, L Q.]] |
[[Category: Li, J.]] | [[Category: Li, J.]] | ||
[[Category: Liu, F.]] | [[Category: Liu, F.]] | ||
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[[Category: ph domain]] | [[Category: ph domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:12:11 2008'' |
Revision as of 15:12, 21 February 2008
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Crystal Structure of the BAR-PH domain of human APPL1
Overview
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.
About this Structure
2ELB is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structures of the BAR-PH and PTB domains of human APPL1., Li J, Mao X, Dong LQ, Liu F, Tong L, Structure. 2007 May;15(5):525-33. PMID:17502098
Page seeded by OCA on Thu Feb 21 17:12:11 2008
Categories: Homo sapiens | Single protein | Dong, L Q. | Li, J. | Liu, F. | Mao, X. | Tong, L. | Appl | Bar domain | Ph domain
