Structural and Membrane Binding Analysis of the PX Domain of Bem1p: Basis of Phosphatidylinositol-4-Phosphate Specificity*
نویسندگان
چکیده
From the Departments of Chemistry, University of Illinois at Chicago, Chicago, IL 60607, USA, the Department of Biochemistry and Molecular Biology, Indiana University School of Medicine-South Bend and the Department of Chemistry and Biochemistry and the Walther Center for Cancer Research, University of Notre Dame, South Bend, IN 46617, USA, MRC Laboratory of Molecular Biology, Cambridge CB2 2QH, UK, and the Department of Microbiology and Immunology, Weill Medical College of Cornell University, New York, NY 10021, USA
منابع مشابه
Structural and membrane binding analysis of the Phox homology domain of Bem1p: basis of phosphatidylinositol 4-phosphate specificity.
Phox homology (PX) domains, which have been identified in a variety of proteins involved in cell signaling and membrane trafficking, have been shown to interact with phosphoinositides (PIs) with different affinities and specificities. To elucidate the structural origin of the diverse PI specificity of PX domains, we determined the crystal structure of the PX domain from Bem1p that has been repo...
متن کاملStructural and Membrane Binding Analysis of the PX Domain of Phosphoinositide 3-Kinase-C2α*
Phox homology (PX) domains, which have been identified in a variety of proteins involved in cell signaling and membrane trafficking, have been shown to interact with phosphoinositides (PIs) with different affinities and specificities. To elucidate the structural origin of diverse PI specificities of PX domains, we determined the crystal structure of the PX domain from phosphoinositide 3-kinase ...
متن کاملThe crystal structure of the PX domain from p40(phox) bound to phosphatidylinositol 3-phosphate.
More than 50 human proteins with a wide range of functions have a 120 residue phosphoinositide binding module known as the PX domain. The 1.7 A X-ray crystal structure of the PX domain from the p40(phox) subunit of NADPH oxidase bound to PtdIns(3)P shows that the PX domain embraces the 3-phosphate on one side of a water-filled, positively charged pocket and reveals how 3-phosphoinositide specif...
متن کاملStructural basis for different phosphoinositide specificities of the PX domains of sorting nexins regulating G-protein signaling.
Sorting nexins (SNXs) or phox homology (PX) domain containing proteins are central regulators of cell trafficking and signaling. A subfamily of PX domain proteins possesses two unique PX-associated domains, as well as a regulator of G protein-coupled receptor signaling (RGS) domain that attenuates Gαs-coupled G protein-coupled receptor signaling. Here we delineate the structural organization of...
متن کاملStructural basis for PI(4)P-specific membrane recruitment of the Legionella pneumophila effector DrrA/SidM.
Recruitment of the Legionella pneumophila effector DrrA to the Legionella-containing vacuole, where it activates and AMPylates Rab1, is mediated by a P4M domain that binds phosphatidylinositol 4-phosphate [PI(4)P] with high affinity and specificity. Despite the importance of PI(4)P in Golgi trafficking and its manipulation by pathogens, the structural bases for PI(4)P-dependent membrane recruit...
متن کامل