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金鱼草中心辐射蛋白(CEN)的结构表明其具有激酶调节因子的作用。

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

作者信息

Banfield M J, Brady R L

机构信息

Department of Biochemistry, University of Bristol, Bristol, BS8 1TD, UK.

出版信息

J Mol Biol. 2000 Apr 14;297(5):1159-70. doi: 10.1006/jmbi.2000.3619.

DOI:10.1006/jmbi.2000.3619
PMID:10764580
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.

摘要

植物蛋白辐射对称基因(CEN)的表达会导致茎生长与花结构(花序)发育之间的形态转换。我们已经确定了金鱼草CEN的晶体结构,分辨率为1.9埃。该结构证实,正如从序列同源性预测的那样,CEN蛋白是磷脂酰乙醇胺结合蛋白(PEBP)家族的一个子集。已发现哺乳动物形式的PEBP可作为丝裂原活化蛋白激酶信号传导的抑制剂,丝裂原活化蛋白激酶信号传导是调节细胞分化的核心信号级联反应。CEN和PEBP蛋白具有相似的拓扑结构,以一个大的中央β折叠为主。在该折叠一端的一个能够结合磷酸化配体的结合口袋高度保守,这表明CEN与PEBP一样,其生物学效应源于该区域与磷酸化配体形成复合物的能力,从而干扰激酶及其效应器。

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