Structural highlights
FunctionCEN_ANTMA Expression of CEN leads to a morphological switch between shoot growth and the development of flower structures (inflorescence). May form complexes with phosphorylated ligands by interfering with kinases and their effectors. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedExpression 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 A 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 beta-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. The structure of Antirrhinum centroradialis protein (CEN) suggests a role as a kinase regulator.,Banfield MJ, Brady RL J Mol Biol. 2000 Apr 14;297(5):1159-70. PMID:10764580[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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