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PDBsum entry 1ghq
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Immune system/viral protein receptor
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PDB id
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1ghq
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structure of complement receptor 2 in complex with its c3d ligand.
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Authors
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G.Szakonyi,
J.M.Guthridge,
D.Li,
K.Young,
V.M.Holers,
X.S.Chen.
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Ref.
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Science, 2001,
292,
1725-1728.
[DOI no: ]
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PubMed id
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Abstract
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Complement receptor 2 (CR2/CD21) is an important receptor that amplifies B
lymphocyte activation by bridging the innate and adaptive immune systems. CR2
ligands include complement C3d and Epstein-Barr virus glycoprotein 350/220. We
describe the x-ray structure of this CR2 domain in complex with C3d at 2.0
angstroms. The structure reveals extensive main chain interactions between C3d
and only one short consensus repeat (SCR) of CR2 and substantial SCR side-side
packing. These results provide a detailed understanding of receptor-ligand
interactions in this protein family and reveal potential target sites for
molecular drug design.
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Figure 3.
Fig. 3. Structure at the CR2-C3d interface. (A and B) Surface
features of the interface area on C3d (in cyan) and CR2 molecule
(in yellow). The shape of the interface of one molecule
complements that of the other (prepared using GRASP). (C)
Structure of the CR2 SCR2 (yellow) and C3d (cyan) complex. (D
and E) The detailed interactions between CR2 (yellow) and C3d
(cyan) in two angles. Dashed lines represent H-bonds between
carbonyl oxygen atoms (red), nitrogen atoms (blue) of amino acid
side chains or main chain, and water molecules (pink).
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Figure 4.
Fig. 4. ELISA results demonstrating the relative inhibition of
binding of full-length soluble CR2 at 2 µg/ml to
plate-bound C3d by wild-type C3d (wt) compared to mutant C3d
(mut1, mut2, and mut4) at several concentrations. Wt and mut1
inhibited CR2-C3d binding similarly, whereas mut2 and mut4 have
lost most of their inhibitory capabilities and, thus, do not
effectively interact with CR2.
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The above figures are
reprinted
by permission from the AAAs:
Science
(2001,
292,
1725-1728)
copyright 2001.
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