Overproduction, purification and preliminary crystallographic analysis of the carbohydrate-recognition domain of human langerin.
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.
Thépaut
Michel
M
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.
Vivès
Corinne
C
Pompidor
Guillaume
G
Kahn
Richard
R
Fieschi
Franck
F
D015703:Antigens, CD / Q000737:chemistry* / Q000302:isolation & purification; D001483:Base Sequence; D002241:Carbohydrates / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D017931:DNA Primers; D006801:Humans; D037181:Lectins, C-Type / Q000737:chemistry* / Q000302:isolation & purification; D037241:Mannose-Binding Lectins / Q000737:chemistry* / Q000302:isolation & purification
D015703:Antigens, CD; C121916:CD207 protein, human; D002241:Carbohydrates; D017931:DNA Primers; D037181:Lectins, C-Type; D037241:Mannose-Binding Lectins