4mx3

Crystal Structure of PKA RIalpha HomodimerCrystal Structure of PKA RIalpha Homodimer

Structural highlights 4mx3 is a 2 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.88Å Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function KAP0_BOVIN Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Publication Abstract from PubMed The regulatory (R) subunit is the cAMP receptor of protein kinase A. Following cAMP binding, the inactive PKA holoenzyme complex separates into two active catalytic (C) subunits and a cAMP-bound R dimer. Thus far, only monomeric R structures have been solved, which fell short in explaining differences of cAMP binding for the full-length protein as compared to the truncated R subunits. Here we solved a full-length R-dimer structure that reflects the biologically relevant conformation, and this structure agrees well with small angle X-ray scattering. An isoform-specific interface is revealed between the protomers. This interface acts as an intermolecular sensor for cAMP and explains the cooperative character of cAMP binding to the RIalpha dimer. Mutagenesis of residues on this interface not only leads to structural and biochemical changes, but is also linked to Carney complex disease. PKA RIalpha Homodimer Structure Reveals an Intermolecular Interface with Implications for Cooperative cAMP Binding and Carney Complex Disease.,Bruystens JG, Wu J, Fortezzo A, Kornev AP, Blumenthal DK, Taylor SS Structure. 2014 Jan 7;22(1):59-69. doi: 10.1016/j.str.2013.10.012. Epub 2013 Dec , 5. PMID:24316401 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also CAMP-dependent protein kinase 3D structures

spinqualitylabelsall models 4mx3, resolution 3.88Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image