Idioma:

Conformational flexibility of the complete catalytic domain of Cdc25B phosphatases

Sayegh, Raphael S. R. ; Tamaki, Fabio K. ; Marana, Sandro R. ; Salinas, Roberto K. ; Arantes, Guilherme M.

Proteins, structure, function, and bioinformatics, 2016-11, Vol.84 (11), p.1567-1575 [Periódico revisado por pares]

United States: Blackwell Publishing Ltd

Texto completo disponível

Citações Citado por

Enviar para

Título:
Conformational flexibility of the complete catalytic domain of Cdc25B phosphatases
Autor: Sayegh, Raphael S. R. ; Tamaki, Fabio K. ; Marana, Sandro R. ; Salinas, Roberto K. ; Arantes, Guilherme M.
Assuntos: Amino Acid Motifs ; Catalytic Domain ; cdc25 Phosphatases - chemistry ; cdc25 Phosphatases - genetics ; cdc25 Phosphatases - metabolism ; Cloning, Molecular ; computer simulation ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Gene Expression ; Humans ; molecular dynamics ; Molecular Dynamics Simulation ; NMR spectroscopy ; Nuclear Magnetic Resonance, Biomolecular ; Pliability ; protein dynamics ; protein phosphatase ; Protein Stability ; Protein Structure, Secondary ; Recombinant Fusion Proteins - chemistry ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism
É parte de: Proteins, structure, function, and bioinformatics, 2016-11, Vol.84 (11), p.1567-1575
Notas: CNPq and FAPESP projects - No. 12/00543-1, 08/55914-9, 14/19439-5, 13/17883-2, 14/21900-2
ArticleID:PROT25100
ark:/67375/WNG-8673PLXR-G
istex:9C809C50A68C96FDE4CBBB5D012B2E51E9F29549
S.R.M. and G.M.A. are CNPq research fellows.
The authors declare no conflict of interests.
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Descrição: ABSTRACT Cdc25B phosphatases are involved in cell cycle checkpoints and have become a possible target for developing new anticancer drugs. A more rational design of Cdc25B ligands would benefit from detailed knowledge of its tertiary structure. The conformational flexibility of the C‐terminal region of the Cdc25B catalytic domain has been debated recently and suggested to play an important structural role. Here, a combination of experimental NMR measurements and molecular dynamics simulations for the complete catalytic domain of the Cdc25B phosphatase is presented. The stability of the C‐terminal α‐helix is confirmed, but the last 20 residues in the complete catalytic domain are very flexible, partially occlude the active site and may establish transient contacts with the protein core. This flexibility in the C‐terminal tail may modulate the molecular recognition of natural substrates and competitive inhibitors by Cdc25B. Proteins 2016; 84:1567–1575. © 2016 Wiley Periodicals, Inc.
Editor: United States: Blackwell Publishing Ltd
Idioma: Inglês

Links

View this record in MEDLINE/PubMed

Voltar para lista de resultados

Anterior Resultado 4 Avançar Ir para próxima página

Realização: Logos de Redes Sociais:

Conformational flexibility of the complete catalytic domain of Cdc25B phosphatases

Sayegh, Raphael S. R. ; Tamaki, Fabio K. ; Marana, Sandro R. ; Salinas, Roberto K. ; Arantes, Guilherme M.

United States: Blackwell Publishing Ltd

Buscando em bases de dados remotas. Favor aguardar.