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3jqh
From Proteopedia
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{{STRUCTURE_3jqh| PDB=3jqh | SCENE= }} | {{STRUCTURE_3jqh| PDB=3jqh | SCENE= }} | ||
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===Structure of the neck region of the glycan-binding receptor DC-SIGNR=== | ===Structure of the neck region of the glycan-binding receptor DC-SIGNR=== | ||
| + | {{ABSTRACT_PUBMED_19835887}} | ||
| - | + | ==Function== | |
| - | + | [[http://www.uniprot.org/uniprot/CLC4M_HUMAN CLC4M_HUMAN]] Probable pathogen-recognition receptor involved in peripheral immune surveillance in liver. May mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. Probably recognizes in a calcium-dependent manner high mannose N-linked oligosaccharides in a variety of pathogen antigens, including HIV-1 gp120, HIV-2 gp120, SIV gp120, ebolavirus glycoproteins, HCV E2, and human SARS coronavirus protein S. Is a receptor for ICAM3, probably by binding to mannose-like carbohydrates. Is presumably a coreceptor for the SARS coronavirus.<ref>PMID:11257134</ref><ref>PMID:11226297</ref> | |
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==About this Structure== | ==About this Structure== | ||
| - | + | [[3jqh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JQH OCA]. | |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:019835887</ref><references group="xtra"/><references/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Drickamer, K.]] | [[Category: Drickamer, K.]] | ||
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[[Category: Tso, C K.W.]] | [[Category: Tso, C K.W.]] | ||
[[Category: Weis, W I.]] | [[Category: Weis, W I.]] | ||
| - | [[Category: Alternative splicing]] | ||
| - | [[Category: Calcium]] | ||
[[Category: Cell membrane]] | [[Category: Cell membrane]] | ||
[[Category: Dc-signr]] | [[Category: Dc-signr]] | ||
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[[Category: Metal-binding]] | [[Category: Metal-binding]] | ||
[[Category: Oligomerization domain]] | [[Category: Oligomerization domain]] | ||
| - | [[Category: Polymorphism]] | ||
[[Category: Receptor]] | [[Category: Receptor]] | ||
[[Category: Secreted]] | [[Category: Secreted]] | ||
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[[Category: Sugar binding protein]] | [[Category: Sugar binding protein]] | ||
[[Category: Transmembrane]] | [[Category: Transmembrane]] | ||
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Revision as of 09:18, 27 March 2013
Contents |
Structure of the neck region of the glycan-binding receptor DC-SIGNR
Template:ABSTRACT PUBMED 19835887
Function
[CLC4M_HUMAN] Probable pathogen-recognition receptor involved in peripheral immune surveillance in liver. May mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. Probably recognizes in a calcium-dependent manner high mannose N-linked oligosaccharides in a variety of pathogen antigens, including HIV-1 gp120, HIV-2 gp120, SIV gp120, ebolavirus glycoproteins, HCV E2, and human SARS coronavirus protein S. Is a receptor for ICAM3, probably by binding to mannose-like carbohydrates. Is presumably a coreceptor for the SARS coronavirus.[1][2]
About this Structure
3jqh is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Feinberg H, Tso CK, Taylor ME, Drickamer K, Weis WI. Segmented helical structure of the neck region of the glycan-binding receptor DC-SIGNR. J Mol Biol. 2009 Dec 11;394(4):613-20. Epub 2009 Oct 14. PMID:19835887 doi:10.1016/j.jmb.2009.10.006
- ↑ Bashirova AA, Geijtenbeek TB, van Duijnhoven GC, van Vliet SJ, Eilering JB, Martin MP, Wu L, Martin TD, Viebig N, Knolle PA, KewalRamani VN, van Kooyk Y, Carrington M. A dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN)-related protein is highly expressed on human liver sinusoidal endothelial cells and promotes HIV-1 infection. J Exp Med. 2001 Mar 19;193(6):671-8. PMID:11257134
- ↑ Pohlmann S, Soilleux EJ, Baribaud F, Leslie GJ, Morris LS, Trowsdale J, Lee B, Coleman N, Doms RW. DC-SIGNR, a DC-SIGN homologue expressed in endothelial cells, binds to human and simian immunodeficiency viruses and activates infection in trans. Proc Natl Acad Sci U S A. 2001 Feb 27;98(5):2670-5. PMID:11226297 doi:10.1073/pnas.051631398
Categories: Homo sapiens | Drickamer, K. | Feinberg, H. | Taylor, M E. | Tso, C K.W. | Weis, W I. | Cell membrane | Dc-signr | Disulfide bond | Endocytosis | Four-helix bundle | Glycoprotein | Host-virus interaction | Immune response | Lectin | Mannose-binding | Membrane | Metal-binding | Oligomerization domain | Receptor | Secreted | Signal-anchor | Sugar binding protein | Transmembrane
