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Literature DB >> 26323294

Structure of the 14-3-3ζ-LKB1 fusion protein provides insight into a novel ligand-binding mode of 14-3-3.

Abstract

The 14-3-3 proteins are a family of highly conserved proteins that play key roles in many cellular processes. The tumour suppressor LKB1 regulates cell polarity, cell growth and energy metabolism. 14-3-3 proteins bind to LKB1 and suppress its functions. Previously, preliminary crystallographic data for the 14-3-3ζ-LKB1 fusion protein have been reported. Here, the crystal structure of this fusion protein was solved and a novel potential binding mode of 14-3-3 to its ligands was found.

Entities: Disease Gene

Keywords: 14-3-3ζ; LKB1; crystal structure; tumour supressors

Mesh：

Substances：

Year: 2015 PMID： 26323294 PMCID： PMC4555915 DOI： 10.1107/S2053230X15012595

Source DB: PubMed Journal: Acta Crystallogr F Struct Biol Commun ISSN： 2053-230X Impact factor: 1.056

35 in total

1. C-terminal recognition by 14-3-3 proteins for surface expression of membrane receptors.

Authors: Brian Coblitz; Sojin Shikano; Meng Wu; Sandra B Gabelli; Lisa M Cockrell; Matt Spieker; Yoshiro Hanyu; Haian Fu; L Mario Amzel; Min Li
Journal: J Biol Chem Date: 2005-08-24 Impact factor: 5.157

2. Phosphorylation-independent interaction between 14-3-3 and exoenzyme S: from structure to pathogenesis.

Authors: Christian Ottmann; Lubna Yasmin; Michael Weyand; Jeffrey L Veesenmeyer; Maureen H Diaz; Ruth H Palmer; Matthew S Francis; Alan R Hauser; Alfred Wittinghofer; Bengt Hallberg
Journal: EMBO J Date: 2007-01-18 Impact factor: 11.598

Review 3. 14-3-3 Proteins: diverse functions in cell proliferation and cancer progression.

Authors: Alyson K Freeman; Deborah K Morrison
Journal: Semin Cell Dev Biol Date: 2011-08-22 Impact factor: 7.727

Review 4. AMPK: a nutrient and energy sensor that maintains energy homeostasis.

Authors: D Grahame Hardie; Fiona A Ross; Simon A Hawley
Journal: Nat Rev Mol Cell Biol Date: 2012-03-22 Impact factor: 94.444

5. Features and development of Coot.

Authors: P Emsley; B Lohkamp; W G Scott; K Cowtan
Journal: Acta Crystallogr D Biol Crystallogr Date: 2010-03-24

6. 14-3-3 interacts with LKB1 via recognizing phosphorylated threonine 336 residue and suppresses LKB1 kinase function.

Authors: Yu Bai; Tao Zhou; Haian Fu; Hanyan Sun; Bei Huang
Journal: FEBS Lett Date: 2012-03-23 Impact factor: 4.124

Review 7. LKB1-dependent signaling pathways.

Authors: Dario R Alessi; Kei Sakamoto; Jose R Bayascas
Journal: Annu Rev Biochem Date: 2006 Impact factor: 23.643

8. Towards automated crystallographic structure refinement with phenix.refine.

Authors: Pavel V Afonine; Ralf W Grosse-Kunstleve; Nathaniel Echols; Jeffrey J Headd; Nigel W Moriarty; Marat Mustyakimov; Thomas C Terwilliger; Alexandre Urzhumtsev; Peter H Zwart; Paul D Adams
Journal: Acta Crystallogr D Biol Crystallogr Date: 2012-03-16

Structure of the 14-3-3ζ-LKB1 fusion protein provides insight into a novel ligand-binding mode of 14-3-3.

1. C-terminal recognition by 14-3-3 proteins for surface expression of membrane receptors.

2. Phosphorylation-independent interaction between 14-3-3 and exoenzyme S: from structure to pathogenesis.

Review 3. 14-3-3 Proteins: diverse functions in cell proliferation and cancer progression.

Review 4. AMPK: a nutrient and energy sensor that maintains energy homeostasis.

5. Features and development of Coot.

6. 14-3-3 interacts with LKB1 via recognizing phosphorylated threonine 336 residue and suppresses LKB1 kinase function.

Review 7. LKB1-dependent signaling pathways.

8. Towards automated crystallographic structure refinement with phenix.refine.

9. Structure of the LKB1-STRAD-MO25 complex reveals an allosteric mechanism of kinase activation.

10. Phaser crystallographic software.

1. Chimeric 14-3-3 proteins for unraveling interactions with intrinsically disordered partners.

2. Rac1 S71 Mediates the Interaction between Rac1 and 14-3-3 Proteins.