The Gal/GalNAc-specific lectin from the plant pathogenic basidiomycete Rhizoctonia solani is a member of the ricin-B family
The Gal/GalNAc-specific lectin from the plant pathogenic basidiomycete Rhizoctonia solani is a member of the ricin-B family
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DOI：
10.1006/bbrc.2001.4626
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发表时间：
2001-04-06
影响因子：
3.1
通讯作者：
Rougé, P
中科院分区：
文献类型：
--
作者：
Candy, L;Peumans, WJ;Rougé, P
从植物病原菌solani Rhizoctonia （RSA）中分离出的凝集素是两个15.5 kDa的非共价结合单体的同二聚体，RSA是一个主要由β -片组成的碱性蛋白（pI bbb9）， RSA的n端序列与蓖麻蛋白b的n端亚结构域相似，证实了其与蓖麻蛋白b的关系，疏水性聚类分析证实了这两个蛋白的n端具有相似的折叠。RSA对Gal/GalNAc表现出特异性，其中pyranose环的C3 ‘, C4 ’和C6 '位置的羟基在与单糖的相互作用中起关键作用。我们的研究结果证明了真菌和植物凝集素之间存在明显的进化关系，同时也为蓖麻毒素b的一个亚基组成的凝集素的存在提供了证据。(C) 2001学术出版社。
The lectin isolated from the phytopathogenic basidiomycete Rhizoctonia solani (RSA) is a homodimer of two noncovalently associated monomers of 15.5 kDa, RSA is a basic protein (pI > 9) which consists mainly of beta -sheets, A presumed relationship with ricin-B is supported by the sequence similarity between the N-terminus of RSA and the N-terminal subdomain of ricin-B, Hydrophobic cluster analysis confirms that the N-terminus of both proteins has a comparable folding. RSA exhibits specificity towards Gal/GalNAc whereby the hydroxyls at the C3 ', C4 ', and C6 ' positions of the pyranose ring play a key role in the interaction with simple sugars. The carbohydrate-binding site of RSA apparently accommodates only a single sugar unit, Our results demonstrate an obvious evolutionary relationship between some fungal and plant lectins, but also provide evidence for the occurrence of a lectin consisting of subunits corresponding to a single subdomain of ricin-B. (C) 2001 Academic Press.