Thépaut Michel, Vivès Corinne, Pompidor Guillaume, Kahn Richard, Fieschi Franck
Laboratoire des Protéines Membranaires, Institut de Biologie Structurale Jean-Pierre Ebel, UMR 5075 CNRS/CEA/Université Joseph Fourier, 41 Rue Jules Horowitz, 38027 Grenoble CEDEX, France.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Feb 1;64(Pt 2):115-8. doi: 10.1107/S1744309108001000. Epub 2008 Jan 31.
Langerin, a lectin that is specific to Langerhans cells, interacts with glycoconjugates through its carbohydrate-recognition domain (CRD). This carbohydrate binding occurs by an avidity-based mechanism that is enabled by the neck domain responsible for trimerization. Langerin binds HIV through its CRD and thus plays a protective role against its propagation by the internalization of virions in Birbeck granules. Here, the overproduction, purification and crystallization of the langerin CRD is reported. Crystals obtained by the hanging-drop vapour-diffusion method allowed the collection of a complete data set to 1.5 A resolution and belonged to the tetragonal space group P4(2), with unit-cell parameters a = b = 79.55, c = 90.14 A.
朗格汉斯细胞特异性凝集素（Langerin）通过其碳水化合物识别结构域（CRD）与糖缀合物相互作用。这种碳水化合物结合通过基于亲和力的机制发生，该机制由负责三聚化的颈部结构域促成。Langerin通过其CRD结合HIV，从而通过将病毒粒子内化到伯贝克颗粒中对其传播起到保护作用。在此，报道了Langerin CRD的过量表达、纯化和结晶。通过悬滴气相扩散法获得的晶体能够收集到分辨率为1.5 Å的完整数据集，属于四方晶系空间群P4(2)，晶胞参数a = b = 79.55，c = 90.14 Å。
