Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 64, Issue -, Pages 115-118Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309108001000
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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 angstrom resolution and belonged to the tetragonal space group P4(2), with unit-cell parameters a = b = 79.55, c = 90.14 angstrom.
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