9dw4: Difference between revisions
New page: '''Unreleased structure''' The entry 9dw4 is ON HOLD Authors: Fiedorczuk, K., Chen, J., Csanady, L. Description: Dephosphorylated CFTR in 1:1 complex with PKA-C (site II) [[Category: U... |
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==Dephosphorylated CFTR in 1:1 complex with PKA-C (site II)== | |||
<StructureSection load='9dw4' size='340' side='right'caption='[[9dw4]], [[Resolution|resolution]] 9.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9dw4]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9DW4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9DW4 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 9Å</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9dw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9dw4 OCA], [https://pdbe.org/9dw4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9dw4 RCSB], [https://www.ebi.ac.uk/pdbsum/9dw4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9dw4 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:39495916</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 9dw4" style="background-color:#fffaf0;"></div> | ||
[[Category: Chen | == References == | ||
[[Category: Csanady | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bos taurus]] | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Chen J]] | |||
[[Category: Csanady L]] | |||
[[Category: Fiedorczuk K]] | |||
Latest revision as of 10:51, 21 November 2024
Dephosphorylated CFTR in 1:1 complex with PKA-C (site II)Dephosphorylated CFTR in 1:1 complex with PKA-C (site II)
Structural highlights
Publication Abstract from PubMedProtein 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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