This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

3p5d

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 14:18, 5 August 2016

Structure of the carbohydrate-recognition domain of human Langerin with man5 (Man alpha1-3(Man alpha1-6)Man alpha1-6)(Man- alpha1-3)Man

Structural highlights

3p5d is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	3p5e, 3p5f, 3p5g, 3p5h, 3p5i
Gene:	CD207, CLEC4K (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[CLC4K_HUMAN] Defects in CD207 are the cause of Birbeck granule deficiency (BIRGD) [MIM:613393]. It is a condition characterized by the absence of Birbeck granules in epidermal Langerhans cells. Despite the lack of Birbeck granules Langerhans cells are present in normal numbers and have normal morphologic characteristics and antigen-presenting capacity.^[1] ^[2]

Function

[CLC4K_HUMAN] Calcium-dependent lectin displaying mannose-binding specificity. Induces the formation of Birbeck granules (BGs); is a potent regulator of membrane superimposition and zippering. Binds to sulfated as well as mannosylated glycans, keratan sulfate (KS) and beta-glucans. Facilitates uptake of antigens and is involved in the routing and/or processing of antigen for presentation to T cells. Major receptor on primary Langerhans cells for Candida species, Saccharomyces species, and Malassezia furfur. Protects against human immunodeficiency virus-1 (HIV-1) infection. Binds to high-mannose structures present on the envelope glycoprotein which is followed by subsequent targeting of the virus to the Birbeck granules leading to its rapid degradation.^[3] ^[4] ^[5] ^[6]

Publication Abstract from PubMed

Langerin mediates the carbohydrate-dependent uptake of pathogens by Langerhans cells in the first step of antigen presentation to the adaptive immune system. Langerin binds to an unusually diverse number of endogenous and pathogenic cell surface carbohydrates, including mannose-containing Ospecific polysaccharides derived from bacterial lipopolysaccharides identified here by probing a microarray of bacterial polysaccharides. Crystal structures of the carbohydrate-recognition domain from human langerin bound to a series of oligomannose compounds, the blood group B antigen, and a fragment of beta-glucan reveal binding to mannose, fucose, and glucose residues by Ca(2+) coordination of vicinal hydroxyl groups with similar stereochemistry. Oligomannose compounds bind through a single-mannose residue, with no other mannose residues contacting the protein directly. There is no evidence for a second Ca(2+)-independent binding site. Likewise, a beta-glucan fragment, Glcbeta1-3Glcbeta1-3Glc, binds to langerin through the interaction of a single-glucose residue with the Ca(2+) site. The fucose moiety of the blood group B trisaccharide Galalpha1-3(Fucalpha1-2)Gal also binds to the Ca(2+) site, and selective binding to this glycan compared to other fucose-containing oligosaccharides results from additional favorable interactions of the nonreducing terminal galactose, as well as of the fucose residue. Surprisingly, the equatorial 3-OH group and the axial 4-OH group of the galactose residue in 6SO(4)-Galbeta1-4GlcNAc also coordinate Ca(2+), a heretofore unobserved mode of galactose binding in a C-type carbohydrate-recognition domain bearing the Glu-Pro-Asn signature motif characteristic of mannose binding sites. Salt bridges between the sulfate group and two lysine residues appear to compensate for the nonoptimal binding of galactose at this site.

Structural Basis for Langerin Recognition of Diverse Pathogen and Mammalian Glycans through a Single Binding Site.,Feinberg H, Taylor ME, Razi N, McBride R, Knirel YA, Graham SA, Drickamer K, Weis WI J Mol Biol. 2010 Nov 26. PMID:21112338^[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Verdijk P, Dijkman R, Plasmeijer EI, Mulder AA, Zoutman WH, Mieke Mommaas A, Tensen CP. A lack of Birbeck granules in Langerhans cells is associated with a naturally occurring point mutation in the human Langerin gene. J Invest Dermatol. 2005 Apr;124(4):714-7. PMID:15816828 doi:10.1111/j.0022-202X.2005.23645.x
↑ Ward EM, Stambach NS, Drickamer K, Taylor ME. Polymorphisms in human langerin affect stability and sugar binding activity. J Biol Chem. 2006 Jun 2;281(22):15450-6. Epub 2006 Mar 27. PMID:16567809 doi:10.1074/jbc.M511502200
↑ Valladeau J, Ravel O, Dezutter-Dambuyant C, Moore K, Kleijmeer M, Liu Y, Duvert-Frances V, Vincent C, Schmitt D, Davoust J, Caux C, Lebecque S, Saeland S. Langerin, a novel C-type lectin specific to Langerhans cells, is an endocytic receptor that induces the formation of Birbeck granules. Immunity. 2000 Jan;12(1):71-81. PMID:10661407
↑ de Witte L, Nabatov A, Pion M, Fluitsma D, de Jong MA, de Gruijl T, Piguet V, van Kooyk Y, Geijtenbeek TB. Langerin is a natural barrier to HIV-1 transmission by Langerhans cells. Nat Med. 2007 Mar;13(3):367-71. Epub 2007 Mar 4. PMID:17334373 doi:10.1038/nm1541
↑ Tateno H, Ohnishi K, Yabe R, Hayatsu N, Sato T, Takeya M, Narimatsu H, Hirabayashi J. Dual specificity of Langerin to sulfated and mannosylated glycans via a single C-type carbohydrate recognition domain. J Biol Chem. 2010 Feb 26;285(9):6390-400. doi: 10.1074/jbc.M109.041863. Epub 2009, Dec 21. PMID:20026605 doi:10.1074/jbc.M109.041863
↑ de Jong MA, Vriend LE, Theelen B, Taylor ME, Fluitsma D, Boekhout T, Geijtenbeek TB. C-type lectin Langerin is a beta-glucan receptor on human Langerhans cells that recognizes opportunistic and pathogenic fungi. Mol Immunol. 2010 Mar;47(6):1216-25. doi: 10.1016/j.molimm.2009.12.016. Epub 2010, Jan 25. PMID:20097424 doi:10.1016/j.molimm.2009.12.016
↑ Feinberg H, Taylor ME, Razi N, McBride R, Knirel YA, Graham SA, Drickamer K, Weis WI. Structural Basis for Langerin Recognition of Diverse Pathogen and Mammalian Glycans through a Single Binding Site. J Mol Biol. 2010 Nov 26. PMID:21112338 doi:10.1016/j.jmb.2010.11.039

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3p5d"

@@ Line 1: / Line 1: @@
 ==Structure of the carbohydrate-recognition domain of human Langerin with man5 (Man alpha1-3(Man alpha1-6)Man alpha1-6)(Man- alpha1-3)Man==
 <StructureSection load='3p5d' size='340' side='right' caption='[[3p5d]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3p5d]] is a 4 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=3P5D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3P5D FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3p5d]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P5D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3P5D FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3p5e|3p5e]], [[3p5f|3p5f]], [[3p5g|3p5g]], [[3p5h|3p5h]], [[3p5i|3p5i]]</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CD207, CLEC4K ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CD207, CLEC4K ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3p5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p5d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3p5d RCSB], [http://www.ebi.ac.uk/pdbsum/3p5d PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3p5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p5d OCA], [http://pdbe.org/3p5d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3p5d RCSB], [http://www.ebi.ac.uk/pdbsum/3p5d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3p5d ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 20: / Line 21: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3p5d" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Homo sapiens]]
+[[Category: Human]]
 [[Category: Drickamer, K]]
 [[Category: Feinberg, H]]

3p5d

From Proteopedia

Revision as of 14:18, 5 August 2016

Structure of the carbohydrate-recognition domain of human Langerin with man5 (Man alpha1-3(Man alpha1-6)Man alpha1-6)(Man- alpha1-3)Man

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox