1qou

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1qou, resolution 1.9Å

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CEN (CENTRORADIALIS) PROTEIN FROM ANTIRRHINUM

Overview

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 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.

About this Structure

1QOU is a Single protein structure of sequence from Antirrhinum majus. Full crystallographic information is available from OCA.

Reference

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

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