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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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PDB id:
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| Name: |
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Lipid binding protein
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Title:
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Crystal structure of human complement c3b in complex with smallpox inhibitor of complement (spice)
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Structure:
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Complement c3 beta chain. Chain: a. Fragment: residues 23-667. Synonym: c3 and pzp-like alpha-2-macroglobulin domain-containing protein 1. Complement c3b alpha' chain. Chain: b. Fragment: ccp domains, residues 749-1663. Smallpox inhibitor of complement spice, d15l.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Other_details: purified from human plasma. Variola major virus. Organism_taxid: 12870. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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2.60Å
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R-factor:
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0.199
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R-free:
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0.230
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Authors:
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F.Forneris,J.Wu,X.Xue,P.Gros
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Key ref:
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F.Forneris
et al.
(2016).
Regulators of complement activity mediate inhibitory mechanisms through a common C3b-binding mode.
Embo J,
35,
1133-1149.
PubMed id:
DOI:
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Date:
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18-Nov-15
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Release date:
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06-Apr-16
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PROCHECK
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Headers
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References
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P01024
(CO3_HUMAN) -
Complement C3 from Homo sapiens
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Seq:
Struc:
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1663 a.a.
642 a.a.
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DOI no:
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Embo J
35:1133-1149
(2016)
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PubMed id:
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Regulators of complement activity mediate inhibitory mechanisms through a common C3b-binding mode.
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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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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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Links
