5wxn

Structure of the LKB1 and 14-3-3 complex

spinqualitylabelsall models 5wxn, resolution 2.93Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5wxn is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.93Å Ligands: TPO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 1433Z_HUMAN Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Publication Abstract from PubMed The serine/threonine protein kinase liver kinase B1 (LKB1) is a tumour suppressor and plays important roles in development and metabolism. It phosphorylates AMPK and AMPK-related kinases to regulate multiple physiological processes. Mutations in LKB1 often occur in multiple cancers. LKB1 can be suppressed by 14-3-3 proteins in a phosphorylation-dependent manner. Previously, the structure of a 14-3-3zeta-LKB1 fusion protein has been reported, revealing a phosphorylation-independent binding mode of LKB1 to 14-3-3 proteins. Here, the crystal structure of phosphorylated LKB1 peptide in complex with 14-3-3zeta was solved, which provides a structural basis for the phosphorylation-dependent recognition of LKB1 by 14-3-3 proteins. Structure of the complex of phosphorylated liver kinase B1 and 14-3-3zeta.,Lu Y, Ding S, Zhou R, Wu J Acta Crystallogr F Struct Biol Commun. 2017 Apr 1;73(Pt 4):196-201. doi:, 10.1107/S2053230X17003521. Epub 2017 Mar 22. PMID:28368277 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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