Overproduction, purification and preliminary crystallographic analysis of the carbohydrate-recognition domain of human langerin
Journal Article
·
· Acta Crystallographica. Section F
- 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)
Crystals of the carbohydrate-recognition domain of human langerin were obtained that diffracted synchrotron radiation to 1.5 Å resolution. Langerin, a lectin that is specific to Langerhans cells, interacts with glyco@@conjugates 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 P4{sub 2}, with unit-cell parameters a = b = 79.55, c = 90.14 Å.
- OSTI ID:
- 22363941
- Journal Information:
- Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 2 Vol. 64; ISSN ACSFCL; ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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