The Structure of Physarum polycephalum hemagglutinin I suggests a minimal carbohydrate recognition domain of legume lectin fold.
The Structure of Physarum polycephalum hemagglutinin I suggests a minimal carbohydrate recognition domain of legume lectin fold.
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多头绒泡菌血凝素 I 的结构表明豆类凝集素折叠有一个最小的碳水化合物识别域。
DOI：
10.1016/j.jmb.2010.11.024
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发表时间：
2011
影响因子：
5.6
通讯作者：
K. Kawano
中科院分区：
文献类型：
--
作者：
T. Kouno;N. Watanabe;N. Sakai;Takashi Nakamura;Y. Nabeshima;M. Morita;M. Mizuguchi;T. Aizawa;M. Demura;T. Imanaka;I. Tanaka;K. Kawano
多头绒泡菌血凝素I（HA 1）是一种分泌到细胞外空间的104个残基的蛋白质。HA 1的晶体结构具有在凝集素结构（如豆类凝集素和半乳糖凝集素）中发现的β-夹心折叠。有趣的是，HA 1的β-三明治结构缺乏果冻卷基序，基本上由两个简单的上下β-折叠组成。这种上下β折叠基序在来自动物、植物、细菌和病毒的其他豆类凝集素样蛋白中很好地保守。更值得注意的是，上下β折叠基序包括许多与目标碳水化合物接触的残基。我们的NMR数据表明，HA 1缺乏果冻卷基序也结合到它的目标糖肽。综上所述，这些数据表明，上下β折叠基序为豆科植物凝集素样蛋白与靶糖的结合提供了基本的支架，并且HA 1的结构表明了最小的糖识别结构域。
Physarum polycephalum hemagglutinin I (HA1) is a 104-residue protein that is secreted to extracellular space. The crystal structure of HA1 has a β-sandwich fold found among lectin structures, such as legume lectins and galectins. Interestingly, the β-sandwich of HA1 lacks a jelly roll motif and is essentially composed of two simple up-and-down β-sheets. This up-and-down β-sheet motif is well conserved in other legume lectin-like proteins derived from animals, plants, bacteria, and viruses. It is more noteworthy that the up-and-down β-sheet motif includes many residues that make contact with the target carbohydrates. Our NMR data demonstrate that HA1 lacking a jelly roll motif also binds to its target glycopeptide. Taken together, these data show that the up-and-down β-sheet motif provides a fundamental scaffold for the binding of legume lectin-like proteins to the target carbohydrates, and the structure of HA1 suggests a minimal carbohydrate recognition domain.
牛胎球蛋白 N-连接糖肽的大规模制备和表征。
影响因子：
2.9
作者：
Rice,KG;Rao,NB;Lee,YC
通讯作者：
Lee,YC