Department of Biology and Biochemistry, University of Bath, Claverton Down, Bath BA2 7AY, United Kingdom.
J Biol Chem. 2011 Jun 24;286(25):22243-9. doi: 10.1074/jbc.M111.225755. Epub 2011 May 4.
The CCN (cyr61, ctgf, nov) proteins (CCN1-6) are an important family of matricellular regulatory factors involved in internal and external cell signaling. They are central to essential biological processes such as adhesion, proliferation, angiogenesis, tumorigenesis, wound healing, and modulation of the extracellular matrix. They possess a highly conserved modular structure with four distinct modules that interact with a wide range of regulatory proteins and ligands. However, at the structural level, little is known although their biological function(s) seems to require cooperation between individual modules. Here we present for the first time structural determinants of two of the CCN family members, CCN3 and CCN5 (expressed in Escherichia coli), using small angle x-ray scattering. The results provide a description of the overall molecular shape and possible general three-dimensional modular arrangement for CCN proteins. These data unequivocally provide insight of the nature of CCN protein(s) in solution and thus important insight into their structure-function relationships.
CCN（cyr61、ctgf、nov）蛋白（CCN1-6）是一组重要的细胞外基质调节因子家族，参与细胞内和细胞外的信号转导。它们是细胞黏附、增殖、血管生成、肿瘤发生、创伤愈合和细胞外基质调节等基本生物学过程的核心。它们具有高度保守的模块结构，由四个不同的模块组成，与广泛的调节蛋白和配体相互作用。然而，尽管它们的生物学功能似乎需要各个模块之间的合作，但在结构水平上，人们对此知之甚少。在这里，我们首次使用小角度 X 射线散射技术，对 CCN 家族的两个成员 CCN3 和 CCN5（在大肠杆菌中表达）的结构决定因素进行了研究。研究结果提供了 CCN 蛋白整体分子形状和可能的一般三维模块排列的描述。这些数据明确提供了 CCN 蛋白在溶液中的性质的见解，从而为它们的结构-功能关系提供了重要的见解。
