Departamento de Biologia Molecular, Universidade Federal da Paraíba, campus l, s/n, 58059-900 João Pessoa, Paraíba, Brazil.
Biochimie. 2012 Mar;94(3):900-6. doi: 10.1016/j.biochi.2011.12.009. Epub 2011 Dec 16.
The lectin of Dioclea virgata (DvirL), both native and complexed with X-man, was submitted to X-ray diffraction analysis and the crystal structure was compared to that of other Diocleinae lectins in order to better understand differences in biological properties, especially with regard to the ability of lectins to induce nitric oxide (NO) production. An association was observed between the volume of the carbohydrate recognition domain (CRD), the ability to induce NO production and the relative positions of Tyr12, Arg228 and Leu99. Thus, differences in biological activity induced by Diocleinae lectins are related to the configuration of amino acid residues in the carbohydrate binding site and to the structural conformation of subsequent regions capable of influencing site-ligand interactions. In conclusion, the ability of Diocleinae lectins to induce NO production depends on CRD configuration.
菜豆凝集素（DvirL），不论是天然的还是与 X-man 结合的，都经过了 X 射线衍射分析，其晶体结构与其他 Diocleinae 凝集素进行了比较，以便更好地了解生物学特性的差异，特别是在诱导一氧化氮（NO）产生方面的差异。观察到碳水化合物识别结构域（CRD）的体积、诱导 NO 产生的能力以及 Tyr12、Arg228 和 Leu99 的相对位置之间存在关联。因此，Diocleinae 凝集素诱导的生物学活性的差异与碳水化合物结合位点中氨基酸残基的构型以及能够影响配体相互作用的后续区域的结构构象有关。总之，Diocleinae 凝集素诱导 NO 产生的能力取决于 CRD 结构。
