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

Abstract:

: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.

journal_name

J Mol Biol

authors

Banfield MJ,Brady RL

doi

10.1006/jmbi.2000.3619

keywords:

subject

Has Abstract

pub_date

2000-04-14 00:00:00

pages

1159-70

issue

5

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(00)93619-2

journal_volume

297

pub_type

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