Langerin-heparin interaction: Analysis of the binding to the non-lectin site
Langerin is a C-type lectin involved in the immune response that forms a trimer in its active form. It can interact with carbohydrates using 2 sites with different selectivity, the C-lectin site, a Ca-mediated binding, and the cleft between chains. Here we report the complementary analysis of the in...
| Autores: | , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2019 |
| País: | España |
| Institución: | Consejo Superior de Investigaciones Científicas (CSIC) |
| Repositorio: | DIGITAL.CSIC. Repositorio Institucional del CSIC |
| OAI Identifier: | oai:digital.csic.es:10261/199849 |
| Acceso en línea: | http://hdl.handle.net/10261/199849 |
| Access Level: | acceso abierto |
| Palabra clave: | STD-NMR CORCEMA-ST Langerin Glycosaminoglycan C-type lectin |
| Sumario: | Langerin is a C-type lectin involved in the immune response that forms a trimer in its active form. It can interact with carbohydrates using 2 sites with different selectivity, the C-lectin site, a Ca-mediated binding, and the cleft between chains. Here we report the complementary analysis of the interaction between a heparin-like hexasaccharide 1 and langerin at the second site. |
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