1sl6
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Both the dendritic cell receptor DC-SIGN and the closely related | + | 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== | ==Disease== | ||
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[[Category: Feinberg, H.]] | [[Category: Feinberg, H.]] | ||
[[Category: Guo, Y.]] | [[Category: Guo, Y.]] | ||
| - | [[Category: Mitchell, D | + | [[Category: Mitchell, D A.]] |
| - | [[Category: Taylor, M | + | [[Category: Taylor, M E.]] |
| - | [[Category: Weis, W | + | [[Category: Weis, W I.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: c-type lectin]] | [[Category: c-type lectin]] | ||
[[Category: dc-signr]] | [[Category: dc-signr]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:02:48 2008'' |
Revision as of 13:02, 21 February 2008
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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 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 Thu Feb 21 15:02:48 2008
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
