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PDBsum entry 3wh2
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Immune system
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PDB id
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3wh2
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PDB id:
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| Name: |
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Immune system
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Title:
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Human mincle in complex with citrate
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Structure:
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C-type lectin domain family 4 member e. Chain: a. Fragment: extracellular domain, unp residues 74-219. Synonym: c-type lectin superfamily member 9, macrophage-induciblE C- type lectin. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: clec4e. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.30Å
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R-factor:
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0.129
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R-free:
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0.156
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Authors:
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A.Furukawa,J.Kamishikiryo,D.Mori,K.Toyonaga,Y.Okabe,A.Toji,R.Kanda, Y.Miyake,T.Ose,S.Yamasaki,K.Maenaka
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Key ref:
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A.Furukawa
et al.
(2013).
Structural analysis for glycolipid recognition by the C-type lectins Mincle and MCL.
Proc Natl Acad Sci U S A,
110,
17438-17443.
PubMed id:
DOI:
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Date:
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21-Aug-13
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Release date:
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23-Oct-13
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PROCHECK
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Headers
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References
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Q9ULY5
(CLC4E_HUMAN) -
C-type lectin domain family 4 member E from Homo sapiens
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Seq:
Struc:
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219 a.a.
132 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 1 residue position (black
cross)
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DOI no:
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Proc Natl Acad Sci U S A
110:17438-17443
(2013)
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PubMed id:
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Structural analysis for glycolipid recognition by the C-type lectins Mincle and MCL.
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A.Furukawa,
J.Kamishikiryo,
D.Mori,
K.Toyonaga,
Y.Okabe,
A.Toji,
R.Kanda,
Y.Miyake,
T.Ose,
S.Yamasaki,
K.Maenaka.
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ABSTRACT
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Mincle [macrophage inducible Ca(2+)-dependent (C-type) lectin; CLEC4E] and MCL
(macrophage C-type lectin; CLEC4D) are receptors for the cord factor TDM
(trehalose-6,6'-dimycolate), a unique glycolipid of mycobacterial cell-surface
components, and activate immune cells to confer adjuvant activity. Although it
is known that receptor-TDM interactions require both sugar and lipid moieties of
TDM, the mechanisms of glycolipid recognition by Mincle and MCL remain unclear.
We here report the crystal structures of Mincle, MCL, and the Mincle-citric acid
complex. The structures revealed that these receptors are capable of interacting
with sugar in a Ca(2+)-dependent manner, as observed in other C-type lectins.
However, Mincle and MCL uniquely possess shallow hydrophobic regions found
adjacent to their putative sugar binding sites, which reasonably locate for
recognition of fatty acid moieties of glycolipids. Functional studies using
mutant receptors as well as glycolipid ligands support this deduced binding
mode. These results give insight into the molecular mechanism of glycolipid
recognition through C-type lectin receptors, which may provide clues to rational
design for effective adjuvants.
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Links
