5WXN

Structure of the LKB1 and 14-3-3 complex

Summary for 5WXN

• Entry DOI: 10.2210/pdb5wxn/pdb
• Descriptor: 14-3-3 protein zeta/delta, Serine/threonine-protein kinase STK11 (3 entities in total)
• Functional Keywords: kinase, tumor suppressor, protein complex, protein binding-transferase complex, protein binding/transferase
• Biological source: Homo sapiens (Human); More
• Cellular location: Cytoplasm : P63104; Nucleus. Isoform 2: Nucleus : Q15831
• Total number of polymer chains: 4
• Total formula weight: 64355.96

Authors

Ding, S.,Shi, Z.B. (deposition date: 2017-01-08, release date: 2017-04-19, Last modification date: 2023-11-22)

Primary citation

Lu, Y.,Ding, S.,Zhou, R.,Wu, J.
Structure of the complex of phosphorylated liver kinase B1 and 14-3-3 zeta
Acta Crystallogr F Struct Biol Commun, 73:196-201, 2017

PubMed Abstract: 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 14-3-3ζ-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 14-3-3ζ was solved, which provides a structural basis for the phosphorylation-dependent recognition of LKB1 by 14-3-3 proteins.

PubMed: 28368277
DOI: 10.1107/S2053230X17003521

Experimental method

X-RAY DIFFRACTION (2.93 Å)