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4WMY

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

Summary for 4WMY
Entry DOI10.2210/pdb4wmy/pdb
Related4WMQ
DescriptorIntelectin-1, CALCIUM ION, prop-2-en-1-yl beta-D-galactofuranoside, ... (4 entities in total)
Functional Keywordslectin, disulfide-linked, carbohydrate-binding, innate immunity, calcium, microbe-binding, microbe-specific, galactose, galactofuranose, diol, sugar binding protein
Biological sourceHomo sapiens (Human)
Cellular locationCell membrane; Lipid-anchor, GPI-anchor: Q8WWA0
Total number of polymer chains2
Total formula weight69197.94
Authors
Wangkanont, K.,Kiessling, L.L.,Forest, K.T. (deposition date: 2014-10-09, release date: 2015-07-01, Last modification date: 2024-11-13)
Primary citationWesener, D.A.,Wangkanont, K.,McBride, R.,Song, X.,Kraft, M.B.,Hodges, H.L.,Zarling, L.C.,Splain, R.A.,Smith, D.F.,Cummings, R.D.,Paulson, J.C.,Forest, K.T.,Kiessling, L.L.
Recognition of microbial glycans by human intelectin-1.
Nat.Struct.Mol.Biol., 22:603-610, 2015
Cited by
PubMed Abstract: 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: β-linked D-galactofuranose (β-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-Å-resolution crystal structure of hIntL-1 complexed with β-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.
PubMed: 26148048
DOI: 10.1038/nsmb.3053
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.601 Å)
Structure validation

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