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

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...

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Bibliographic Details
Published in:Journal of molecular biology 2000-04, Vol.297 (5), p.1159-1170
Main Authors: Banfield, M.J, Brady, R.L
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Androgen-Binding Protein
Animals
Antirrhinum majus
binding proteins
Binding Sites
Carrier Proteins - chemistry
Carrier Proteins - metabolism
Cattle
Conserved Sequence
crystal structure
Crystallization
Crystallography, X-Ray
crystals
Dimerization
enzyme inhibitors
Humans
inflorescence control
kinase-inhibitor
Ligands
Models, Biological
Models, Molecular
molecular conformation
Molecular Sequence Data
pdb/1qou
pdb/1qousf
Phosphates - metabolism
Phosphatidylethanolamine Binding Protein
Phospholipid Transfer Proteins
phosphtidylethanolamine
plant proteins
Plant Proteins - chemistry
Plant Proteins - metabolism
Plants - chemistry
Plants - enzymology
Protein Binding
Protein Folding
Protein Kinase Inhibitors
Protein Kinases - metabolism
Protein Structure, Secondary
Sequence Alignment
signalling
Structure-Activity Relationship
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Summary: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.
ISSN:0022-2836
1089-8638
DOI:10.1006/jmbi.2000.3619