1KC5

CRYSTAL STRUCTURE OF ANTIBODY PC287 IN COMPLEX WITH PS1 PEPTIDE

Summary for 1KC5

• Entry DOI: 10.2210/pdb1kc5/pdb
• Related: 1KCR 1KCS 1KCU 1KCV
• Descriptor: PC287 Immunoglobulin, PS1 peptide, ... (4 entities in total)
• Functional Keywords: antibody, peptide antigen, complex (antibody-peptide), immune system
• Biological source: Mus musculus (house mouse); More
• Cellular location: Cell membrane; Single-pass membrane protein (Potential): P01869
• Total number of polymer chains: 3
• Total formula weight: 48269.44

Authors

Nair, D.T.,Singh, K.,Siddiqui, Z.,Nayak, B.P.,Rao, K.V.,Salunke, D.M. (deposition date: 2001-11-07, release date: 2002-07-24, Last modification date: 2024-11-20)

Primary citation

Nair, D.T.,Singh, K.,Siddiqui, Z.,Nayak, B.P.,Rao, K.V.,Salunke, D.M.
Epitope recognition by diverse antibodies suggests conformational convergence in an antibody response.
J.Immunol., 168:2371-2382, 2002

PubMed Abstract: 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.

PubMed: 11859128

Experimental method

X-RAY DIFFRACTION (2.5 Å)