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4wmy

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Revision as of 07:16, 7 April 2023

Structure of Human intelectin-1 in complex with allyl-beta-galactofuranose

Structural highlights

4wmy is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ITLN1_HUMAN Has no effect on basal glucose uptake but enhances insulin-stimulated glucose uptake in adipocytes. Increases AKT phosphorylation in the absence and presence of insulin. May play a role in the defense system against microorganisms. May specifically recognize carbohydrate chains of pathogens and bacterial components containing galactofuranosyl residues, in a calcium-dependent manner. May be involved in iron metabolism.^[1] ^[2]

Publication Abstract from PubMed

The glycans displayed on mammalian cells can differ markedly from those on microbes. Such differences could, in principle, be 'read' by carbohydrate-binding proteins, or lectins. We used glycan microarrays to show that human intelectin-1 (hIntL-1) does not bind known human glycan epitopes but does interact with multiple glycan epitopes found exclusively on microbes: beta-linked D-galactofuranose (beta-Galf), D-phosphoglycerol-modified glycans, heptoses, D-glycero-D-talo-oct-2-ulosonic acid (KO) and 3-deoxy-D-manno-oct-2-ulosonic acid (KDO). The 1.6-A-resolution crystal structure of hIntL-1 complexed with beta-Galf revealed that hIntL-1 uses a bound calcium ion to coordinate terminal exocyclic 1,2-diols. N-acetylneuraminic acid (Neu5Ac), a sialic acid widespread in human glycans, has an exocyclic 1,2-diol but does not bind hIntL-1, probably owing to unfavorable steric and electronic effects. hIntL-1 marks only Streptococcus pneumoniae serotypes that display surface glycans with terminal 1,2-diol groups. This ligand selectivity suggests that hIntL-1 functions in microbial surveillance.

Recognition of microbial glycans by human intelectin-1.,Wesener DA, Wangkanont K, McBride R, Song X, Kraft MB, Hodges HL, Zarling LC, Splain RA, Smith DF, Cummings RD, Paulson JC, Forest KT, Kiessling LL Nat Struct Mol Biol. 2015 Jul 6. doi: 10.1038/nsmb.3053. PMID:26148048^[3]

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

References

↑ Tsuji S, Uehori J, Matsumoto M, Suzuki Y, Matsuhisa A, Toyoshima K, Seya T. Human intelectin is a novel soluble lectin that recognizes galactofuranose in carbohydrate chains of bacterial cell wall. J Biol Chem. 2001 Jun 29;276(26):23456-63. Epub 2001 Apr 19. PMID:11313366 doi:http://dx.doi.org/10.1074/jbc.M103162200
↑ Yang RZ, Lee MJ, Hu H, Pray J, Wu HB, Hansen BC, Shuldiner AR, Fried SK, McLenithan JC, Gong DW. Identification of omentin as a novel depot-specific adipokine in human adipose tissue: possible role in modulating insulin action. Am J Physiol Endocrinol Metab. 2006 Jun;290(6):E1253-61. Epub 2006 Mar 10. PMID:16531507 doi:http://dx.doi.org/00572.2004
↑ Wesener DA, Wangkanont K, McBride R, Song X, Kraft MB, Hodges HL, Zarling LC, Splain RA, Smith DF, Cummings RD, Paulson JC, Forest KT, Kiessling LL. Recognition of microbial glycans by human intelectin-1. Nat Struct Mol Biol. 2015 Jul 6. doi: 10.1038/nsmb.3053. PMID:26148048 doi:http://dx.doi.org/10.1038/nsmb.3053

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4wmy"

Categories: Homo sapiens | Large Structures | Forest KT | Kiessling LL | Wangkanont K

@@ Line 3: / Line 3: @@
 <StructureSection load='4wmy' size='340' side='right'caption='[[4wmy]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4wmy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WMY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WMY FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4wmy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WMY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WMY FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3S6:PROP-2-EN-1-YL+BETA-D-GALACTOFURANOSIDE'>3S6</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4wmq|4wmq]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ITLN1, INTL, ITLN, LFR, UNQ640/PRO1270 ([https://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'>[https://proteopedia.org/fgij/fg.htm?mol=4wmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wmy OCA], [https://pdbe.org/4wmy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wmy RCSB], [https://www.ebi.ac.uk/pdbsum/4wmy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wmy ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/ITLN1_HUMAN ITLN1_HUMAN]] Has no effect on basal glucose uptake but enhances insulin-stimulated glucose uptake in adipocytes. Increases AKT phosphorylation in the absence and presence of insulin. May play a role in the defense system against microorganisms. May specifically recognize carbohydrate chains of pathogens and bacterial components containing galactofuranosyl residues, in a calcium-dependent manner. May be involved in iron metabolism.<ref>PMID:11313366</ref> <ref>PMID:16531507</ref>
+[https://www.uniprot.org/uniprot/ITLN1_HUMAN ITLN1_HUMAN] Has no effect on basal glucose uptake but enhances insulin-stimulated glucose uptake in adipocytes. Increases AKT phosphorylation in the absence and presence of insulin. May play a role in the defense system against microorganisms. May specifically recognize carbohydrate chains of pathogens and bacterial components containing galactofuranosyl residues, in a calcium-dependent manner. May be involved in iron metabolism.<ref>PMID:11313366</ref> <ref>PMID:16531507</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Forest, K T]]
+[[Category: Forest KT]]
-[[Category: Kiessling, L L]]
+[[Category: Kiessling LL]]
-[[Category: Wangkanont, K]]
+[[Category: Wangkanont K]]
-[[Category: Calcium]]
-[[Category: Carbohydrate-binding]]
-[[Category: Diol]]
-[[Category: Disulfide-linked]]
-[[Category: Galactofuranose]]
-[[Category: Galactose]]
-[[Category: Innate immunity]]
-[[Category: Lectin]]
-[[Category: Microbe-binding]]
-[[Category: Microbe-specific]]
-[[Category: Sugar binding protein]]

4wmy

From Proteopedia

Revision as of 07:16, 7 April 2023

Structure of Human intelectin-1 in complex with allyl-beta-galactofuranose

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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