Open AccessOverproduction, purification and preliminary crystallographic analysis of the carbohydrate‐recognition domain of human langerin
Author(s) -
Thépaut Michel,
Vivès Corinne,
Pompidor Guillaume,
Kahn Richard,
Fieschi Franck
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108001000
Subject(s) - langerin , birbeck granules , internalization , microbiology and biotechnology , chemistry , biophysics , crystallography , biology , antigen , biochemistry , immunology , receptor , langerhans cell , dendritic cell
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 Å resolution and belonged to the tetragonal space group P 4 2 , with unit‐cell parameters a = b = 79.55, c = 90.14 Å.