1sl6
From Proteopedia
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Crystal Structure of a fragment of DC-SIGNR (containg the carbohydrate recognition domain and two repeats of the neck) complexed with Lewis-x.
Contents |
Overview
Both the dendritic cell receptor DC-SIGN and the closely related, endothelial cell receptor DC-SIGNR bind human immunodeficiency virus and, enhance infection. However, biochemical and structural comparison of these, receptors now reveals that they have very different physiological, functions. By screening an extensive glycan array, we demonstrated that, DC-SIGN and DC-SIGNR have distinct ligand-binding properties. Our, structural and mutagenesis data explain how both receptors bind, high-mannose oligosaccharides on enveloped viruses and why only DC-SIGN, binds blood group antigens, including those present on microorganisms., DC-SIGN mediates endocytosis, trafficking as a recycling receptor and, releasing ligand at endosomal pH, whereas DC-SIGNR does not release ligand, at low pH or mediate endocytosis. Thus, whereas DC-SIGN has dual, ligand-binding properties and functions both in adhesion and in, endocytosis of pathogens, DC-SIGNR binds a restricted set of ligands and, has only the properties of an adhesion receptor.
Disease
Known disease associated with this structure: SARS infection, protection against OMIM:[605872]
About this Structure
1SL6 is a Single protein structure of sequence from Homo sapiens with CA as ligand. Full crystallographic information is available from OCA.
Reference
Structural basis for distinct ligand-binding and targeting properties of the receptors DC-SIGN and DC-SIGNR., Guo Y, Feinberg H, Conroy E, Mitchell DA, Alvarez R, Blixt O, Taylor ME, Weis WI, Drickamer K, Nat Struct Mol Biol. 2004 Jul;11(7):591-8. Epub 2004 Jun 13. PMID:15195147
Page seeded by OCA on Mon Nov 12 19:15:16 2007
Categories: Homo sapiens | Single protein | Alvarez, R. | Blixt, O. | Conroy, E. | Drickamer, K. | Feinberg, H. | Guo, Y. | Mitchell, D.A. | Taylor, M.E. | Weis, W.I. | CA | C-type lectin | Dc-signr
