2it5

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[[Image:2it5.gif|left|200px]]
[[Image:2it5.gif|left|200px]]
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{{Structure
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|PDB= 2it5 |SIZE=350|CAPTION= <scene name='initialview01'>2it5</scene>, resolution 2.40&Aring;
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The line below this paragraph, containing "STRUCTURE_2it5", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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|GENE= CD209, CLEC4L ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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{{STRUCTURE_2it5| PDB=2it5 | SCENE= }}
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|RELATEDENTRY=[[2it6|2IT6]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2it5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2it5 OCA], [http://www.ebi.ac.uk/pdbsum/2it5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2it5 RCSB]</span>
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'''Crystal Structure of DCSIGN-CRD with man6'''
'''Crystal Structure of DCSIGN-CRD with man6'''
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[[Category: Seeberger, P H.]]
[[Category: Seeberger, P H.]]
[[Category: Weis, W I.]]
[[Category: Weis, W I.]]
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[[Category: c-type lectin]]
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[[Category: C-type lectin]]
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[[Category: protein carbohydrate complex]]
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[[Category: Protein carbohydrate complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:50:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:48:13 2008''
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Revision as of 04:50, 4 May 2008

Template:STRUCTURE 2it5

Crystal Structure of DCSIGN-CRD with man6


Overview

The dendritic cell surface receptor DC-SIGN and the closely related endothelial cell receptor DC-SIGNR specifically recognize high mannose N-linked carbohydrates on viral pathogens. Previous studies have shown that these receptors bind the outer trimannose branch Manalpha1-3[Manalpha1-6]Manalpha present in high mannose structures. Although the trimannoside binds to DC-SIGN or DC-SIGNR more strongly than mannose, additional affinity enhancements are observed in the presence of one or more Manalpha1-2Manalpha moieties on the nonreducing termini of oligomannose structures. The molecular basis of this enhancement has been investigated by determining crystal structures of DC-SIGN bound to a synthetic six-mannose fragment of a high mannose N-linked oligosaccharide, Manalpha1-2Manalpha1-3[Manalpha1-2Manalpha1-6]Manalpha1-6Man and to the disaccharide Manalpha1-2Man. The structures reveal mixtures of two binding modes in each case. Each mode features typical C-type lectin binding at the principal Ca2+-binding site by one mannose residue. In addition, other sugar residues form contacts unique to each binding mode. These results suggest that the affinity enhancement displayed toward oligosaccharides decorated with the Manalpha1-2Manalpha structure is due in part to multiple binding modes at the primary Ca2+ site, which provide both additional contacts and a statistical (entropic) enhancement of binding.

About this Structure

2IT5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Multiple modes of binding enhance the affinity of DC-SIGN for high mannose N-linked glycans found on viral glycoproteins., Feinberg H, Castelli R, Drickamer K, Seeberger PH, Weis WI, J Biol Chem. 2007 Feb 9;282(6):4202-9. Epub 2006 Dec 6. PMID:17150970 Page seeded by OCA on Sun May 4 07:50:15 2008

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