Henrissat B, Popineau Y, Kader J C
Laboratoire de Biochimie et Technologie des Protéines, Institut National de la Recherche Agronomique, Nantes, France.
Biochem J. 1988 Nov 1;255(3):901-5. doi: 10.1042/bj2550901.
Hydrophobic-cluster analysis was used to characterize a conserved domain located near the C-terminal amino acid sequence of wheat (Triticum aestivum) storage proteins. This domain was transformed into a linear template for a global search for similarities in over 5200 protein sequences. In addition to proteins that had already been found to exhibit homology to wheat storage proteins, a previously unreported homology was found with non-specific lipid-transfer proteins from castor bean (Ricinus communis) and from spinach (Spinacia oleracea) leaf. Hydrophobic-cluster analysis of various members of the present protein group clearly shows a typical domain structure where (i) variable and conserved domains are located along the sequence at precise positions, (ii) the conserved domains probably reflect a common ancestor, and (iii) the unique properties of a given protein (chain cut into subunits, repetitive domains, trypsin-inhibitor active site) are associated with the variable domains.
疏水簇分析用于表征位于小麦（普通小麦）贮藏蛋白C末端氨基酸序列附近的一个保守结构域。该结构域被转化为一个线性模板，用于在5200多个蛋白质序列中进行全局相似性搜索。除了已发现与小麦贮藏蛋白具有同源性的蛋白质外，还发现了与蓖麻（蓖麻）和菠菜（菠菜）叶中的非特异性脂质转运蛋白的一种以前未报道的同源性。对本蛋白组不同成员的疏水簇分析清楚地显示了一种典型的结构域结构，其中：（i）可变结构域和保守结构域沿序列位于精确位置，（ii）保守结构域可能反映一个共同祖先，（iii）给定蛋白质的独特性质（链切割成亚基、重复结构域、胰蛋白酶抑制剂活性位点）与可变结构域相关。
