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PDBsum entry 1kcv
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Immune system
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PDB id
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1kcv
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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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Epitope recognition by diverse antibodies suggests conformational convergence in an antibody response.
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Authors
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D.T.Nair,
K.Singh,
Z.Siddiqui,
B.P.Nayak,
K.V.Rao,
D.M.Salunke.
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Ref.
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J Immunol, 2002,
168,
2371-2382.
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PubMed id
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Abstract
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Crystal structures of distinct mAbs that recognize a common epitope of a peptide
Ag have been determined and analyzed in the unbound and bound forms. These Abs
display dissimilar binding site structures in the absence of the Ag. The
dissimilarity is primarily expressed in the conformations of
complementarity-determining region H3, which is responsible for defining the
epitope specificity. Interestingly, however, the three Abs exhibit similar
complementarity-determining region conformations in the Ag binding site while
recognizing the common epitope, indicating that different pathways of binding
are used for Ag recognition. The epitope also exhibits conformational similarity
when bound to each of these Abs, although the peptide Ag was otherwise flexible.
The observed conformational convergence in the epitope and the Ag binding site
was facilitated by the plasticity in the nature of interactions.
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Secondary reference #1
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Title
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Crystal structure of an antibody bound to an immunodominant peptide epitope: novel features in peptide-Antibody recognition.
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Authors
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D.T.Nair,
K.Singh,
N.Sahu,
K.V.Rao,
D.M.Salunke.
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Ref.
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J Immunol, 2000,
165,
6949-6955.
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PubMed id
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