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PDBsum entry 5fob
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Lipid binding protein
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PDB id
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5fob
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Contents |
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642 a.a.
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902 a.a.
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240 a.a.
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References listed in PDB file
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Key reference
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Title
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Regulators of complement activity mediate inhibitory mechanisms through a common c3b-Binding mode.
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Authors
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F.Forneris,
J.Wu,
X.Xue,
D.Ricklin,
Z.Lin,
G.Sfyroera,
A.Tzekou,
E.Volokhina,
J.C.Granneman,
R.Hauhart,
P.Bertram,
M.K.Liszewski,
J.P.Atkinson,
J.D.Lambris,
P.Gros.
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Ref.
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Embo J, 2016,
35,
1133-1149.
[DOI no: ]
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PubMed id
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Abstract
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Regulators of complement activation (RCA) inhibit complement-induced immune
responses on healthy host tissues. We present crystal structures of human RCA
(MCP, DAF, and CR1) and a smallpox virus homolog (SPICE) bound to complement
component C3b. Our structural data reveal that up to four consecutive homologous
CCP domains (i-iv), responsible for inhibition, bind in the same orientation and
extended arrangement at a shared binding platform on C3b. Large sequence
variations in CCP domains explain the diverse C3b-binding patterns, with limited
or no contribution of some individual domains, while all regulators show
extensive contacts with C3b for the domains at the third site. A variation
of ~100° rotation around the longitudinal axis is observed for domains
binding at the fourth site on C3b, without affecting the overall binding mode.
The data suggest a common evolutionary origin for both inhibitory mechanisms,
called decay acceleration and cofactor activity, with variable C3b binding
through domains at sites ii, iii, and iv, and provide a framework for
understanding RCA disease-related mutations and immune evasion.
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