9dw9 | pdb_00009dw9

Phosphorylated (E1371Q)CFTR in complex with PKA-C

spinqualitylabelsall models 9dw9, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9dw9 is a 2 chain structure with sequence from Bos taurus and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.8Å Ligands: ATP, CL, CLR, D10, MG, SEP, TPO, UND Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Protein kinase A (PKA) is a key regulator of cellular functions by selectively phosphorylating numerous substrates, including ion channels, enzymes, and transcription factors. It has long served as a model system for understanding the eukaryotic kinases. Using cryoelectron microscopy, we present complex structures of the PKA catalytic subunit (PKA-C) bound to a full-length protein substrate, the cystic fibrosis transmembrane conductance regulator (CFTR)-an ion channel vital to human health. CFTR gating requires phosphorylation of its regulatory (R) domain. Unphosphorylated CFTR engages PKA-C at two locations, establishing two "catalytic stations" near to, but not directly involving, the R domain. This configuration, coupled with the conformational flexibility of the R domain, permits transient interactions of the eleven spatially separated phosphorylation sites. Furthermore, we determined two structures of the open-pore CFTR stabilized by PKA-C, providing a molecular basis to understand how PKA-C stimulates CFTR currents even in the absence of phosphorylation. The structures of protein kinase A in complex with CFTR: Mechanisms of phosphorylation and noncatalytic activation.,Fiedorczuk K, Iordanov I, Mihalyi C, Szollosi A, Csanady L, Chen J Proc Natl Acad Sci U S A. 2024 Nov 12;121(46):e2409049121. doi: , 10.1073/pnas.2409049121. Epub 2024 Nov 4. PMID:39495916 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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