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PDBsum entry 5a2e
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Immune system
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PDB id
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5a2e
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References listed in PDB file
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Key reference
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Title
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Structures of cd6 and its ligand cd166 give insight into their interaction.
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Authors
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P.E.Chappell,
L.I.Garner,
J.Yan,
C.Metcalfe,
D.Hatherley,
S.Johnson,
C.V.Robinson,
S.M.Lea,
M.H.Brown.
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Ref.
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Structure, 2015,
23,
1426-1436.
[DOI no: ]
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PubMed id
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Abstract
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CD6 is a transmembrane protein with an extracellular region containing three
scavenger receptor cysteine rich (SRCR) domains. The membrane proximal domain of
CD6 binds the N-terminal immunoglobulin superfamily (IgSF) domain of another
cell surface receptor, CD166, which also engages in homophilic interactions. CD6
expression is mainly restricted to T cells, and the interaction between CD6
and CD166 regulates T-cell activation. We have solved the X-ray crystal
structures of the three SRCR domains of CD6 and two N-terminal domains of CD166.
This first structure of consecutive SRCR domains reveals a nonlinear
organization. We characterized the binding sites on CD6 and CD166 and showed
that a SNP in CD6 causes glycosylation that hinders the CD6/CD166 interaction.
Native mass spectrometry analysis showed that there is competition between the
heterophilic and homophilic interactions. These data give insight into how
interactions of consecutive SRCR domains are perturbed by SNPs and potential
therapeutic reagents.
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