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PDBsum entry 2q8a
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Immune system
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PDB id
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2q8a
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Contents |
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316 a.a.
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214 a.a.
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199 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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Structure of the malaria antigen ama1 in complex with a growth-Inhibitory antibody.
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Authors
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A.M.Coley,
A.Gupta,
V.J.Murphy,
T.Bai,
H.Kim,
M.Foley,
R.F.Anders,
A.H.Batchelor.
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Ref.
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Plos Pathog, 2007,
3,
1308-1319.
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PubMed id
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Abstract
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Identifying functionally critical regions of the malaria antigen AMA1 (apical
membrane antigen 1) is necessary to understand the significance of the
polymorphisms within this antigen for vaccine development. The crystal structure
of AMA1 in complex with the Fab fragment of inhibitory monoclonal antibody 1F9
reveals that 1F9 binds to the AMA1 solvent-exposed hydrophobic trough,
confirming its importance. 1F9 uses the heavy and light chain
complementarity-determining regions (CDRs) to wrap around the polymorphic loops
adjacent to the trough, but uses a ridge of framework residues to bind to the
hydrophobic trough. The resulting 1F9-AMA1-combined buried surface of 2,470 A(2)
is considerably larger than previously reported Fab-antigen interfaces.
Mutations of polymorphic AMA1 residues within the 1F9 epitope disrupt 1F9
binding and dramatically reduce the binding of affinity-purified human
antibodies. Moreover, 1F9 binding to AMA1 is competed by naturally acquired
human antibodies, confirming that the 1F9 epitope is a frequent target of
immunological attack.
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