1sl5
From Proteopedia
(New page: 200px<br /> <applet load="1sl5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sl5, resolution 1.80Å" /> '''Crystal Structure o...) |
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caption="1sl5, resolution 1.80Å" /> | caption="1sl5, resolution 1.80Å" /> | ||
'''Crystal Structure of DC-SIGN carbohydrate recognition domain complexed with LNFP III (Dextra L504).'''<br /> | '''Crystal Structure of DC-SIGN carbohydrate recognition domain complexed with LNFP III (Dextra L504).'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1SL5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA and MG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1SL5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SL5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: dc-sign]] | [[Category: dc-sign]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:54:09 2008'' |
Revision as of 14:54, 15 February 2008
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Crystal Structure of DC-SIGN carbohydrate recognition domain complexed with LNFP III (Dextra L504).
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.
About this Structure
1SL5 is a Single protein structure of sequence from Homo sapiens with and as ligands. 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 Fri Feb 15 16:54:09 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 | MG | C-type lectin | Dc-sign
