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PDBsum entry 4n35
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Sugar binding protein
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PDB id
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4n35
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PDB id:
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| Name: |
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Sugar binding protein
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Title:
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Structure of langerin crd i313 complexed with glcnac-beta1-3gal-beta1- 4glc-beta-ch2ch2n3
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Structure:
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C-type lectin domain family 4 member k. Chain: a, b, c, d. Fragment: carbohydrate recognition domain. Synonym: langerin. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: cd207, clec4k. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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1.85Å
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R-factor:
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0.168
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R-free:
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0.212
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Authors:
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H.Feinberg,T.J.W.Rowntree,S.L.W.Tan,K.Drickamer,W.I.Weis,M.E.Taylor
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Key ref:
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H.Feinberg
et al.
(2013).
Common polymorphisms in human langerin change specificity for glycan ligands.
J Biol Chem,
288,
36762-36771.
PubMed id:
DOI:
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Date:
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06-Oct-13
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Release date:
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20-Nov-13
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PROCHECK
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Headers
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References
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Q9UJ71
(CLC4K_HUMAN) -
C-type lectin domain family 4 member K from Homo sapiens
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Seq:
Struc:
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328 a.a.
128 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 2 residue positions (black
crosses)
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DOI no:
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J Biol Chem
288:36762-36771
(2013)
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PubMed id:
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Common polymorphisms in human langerin change specificity for glycan ligands.
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H.Feinberg,
T.J.Rowntree,
S.L.Tan,
K.Drickamer,
W.I.Weis,
M.E.Taylor.
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ABSTRACT
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Langerin, a C-type lectin on Langerhans cells, mediates carbohydrate-dependent
uptake of pathogens in the first step of antigen presentation to the adaptive
immune system. Langerin binds a diverse range of carbohydrates including high
mannose structures, fucosylated blood group antigens, and glycans with terminal
6-sulfated galactose. Mutagenesis and quantitative binding assays indicate that
salt bridges between the sulfate group and two lysine residues compensate for
the nonoptimal binding of galactose at the primary Ca(2+) site. A commonly
occurring single nucleotide polymorphism (SNP) in human langerin results in
change of one of these lysine residues, Lys-313, to isoleucine. Glycan array
screening reveals that this amino acid change abolishes binding to
oligosaccharides with terminal 6SO4-Gal and enhances binding to oligosaccharides
with terminal GlcNAc residues. Structural analysis shows that enhanced binding
to GlcNAc may result from Ile-313 packing against the N-acetyl group. The K313I
polymorphism is tightly linked to another SNP that results in the change N288D,
which reduces affinity for glycan ligands by destabilizing the Ca(2+)-binding
site. Langerin with Asp-288 and Ile-313 shows no binding to 6SO4-Gal-terminated
glycans and increased binding to GlcNAc-terminated structures, but overall
decreased binding to glycans. Altered langerin function in individuals with the
linked N288D and K313I polymorphisms may affect susceptibility to infection by
microorganisms.
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Links
