1kcu: Difference between revisions

Revision as of 14:32, 21 February 2008

CRYSTAL STRUCTURE OF ANTIBODY PC287

OverviewOverview

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.

About this StructureAbout this Structure

1KCU is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Epitope recognition by diverse antibodies suggests conformational convergence in an antibody response., Nair DT, Singh K, Siddiqui Z, Nayak BP, Rao KV, Salunke DM, J Immunol. 2002 Mar 1;168(5):2371-82. PMID:11859128

Page seeded by OCA on Thu Feb 21 13:32:37 2008

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OCA

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 ==Overview==
-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.
+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.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Mus musculus]]
 [[Category: Protein complex]]
-[[Category: Nair, D.T.]]
+[[Category: Nair, D T.]]
-[[Category: Nayak, B.P.]]
+[[Category: Nayak, B P.]]
-[[Category: Rao, K.V.S.]]
+[[Category: Rao, K V.S.]]
-[[Category: Salunke, D.M.]]
+[[Category: Salunke, D M.]]
 [[Category: Siddiqui, Z.]]
 [[Category: Singh, K.]]
 [[Category: anti-peptide antibody]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:12:36 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:32:37 2008''