The structure of Antirrhinum centroradialis protein (CEN) suggests a role as a kinase regulator

M. J. Banfield*, R. L. Brady

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

136 Citations (Scopus)


Expression of the plant protein centroradialis (CEN) leads to a morphological switch between shoot growth and the development of flower structures (inflorescence). We have determined the crystal structure of Antirrhinum CEN to 1.9 Å resolution. This structure confirms the CEN proteins as a subset of the family of phosphatidylethanolamine-binding proteins (PEBP), as predicted from sequence homology. Mammalian forms of PEBP have been found to act as inhibitors of MAP kinase signalling, a central signalling cascade regulating cell differentiation. CEN and PEBP proteins share a similar topology dominated by a large central β-sheet. The strong conservation of a binding pocket at one end of this sheet which is capable of binding phosphoryl ligands, suggests the biological effects of CEN, like PEBP, arise from the ability of this region to form complexes with phosphorylated ligands, hence interfering with kinases and their effectors. (C) 2000 Academic Press.

Original languageEnglish
Pages (from-to)1159-1170
Number of pages12
JournalJournal of Molecular Biology
Issue number5
Publication statusPublished - 14 Apr 2000


  • Inflorescence control
  • Kinase-inhibitor
  • Phosphatidylethanolamine-binding protein
  • Signalling


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