Structure
Volume 1, Issue 2, 15 October 1993, Pages 83-93
Research articleMajor antigen-induced domain rearrangements in an antibody
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Cited by (214)
The Role of the Constant Region in Antibody-Antigen Interactions: Redefining the Modular Model of Immunoglobulin Structure
2018, Structural Biology in Immunology: Structure and Function of Novel Molecules of Immunologic ImportanceConformational heterogeneity in antibody-protein antigen recognition: Implications for high affinity protein complex formation
2014, Journal of Biological ChemistryFrom DARPins to LoopDARPins: Novel LoopDARPin design allows the selection of low picomolar binders in a single round of ribosome display
2014, Journal of Molecular BiologyCitation Excerpt :Nonetheless, structural analysis of different CDR-H3 loops identified common structural patterns within the basis of the loop, although the tip of the loop differed considerably [23,35]. Interestingly, the CDR-H3 loop plays a crucial role in antigen recognition [36,37], sometimes by changing its conformation upon binding [38–40]. The success of the original DARPin design in routinely generating highly specific binders against a multitude of targets with very different properties has been demonstrated in numerous studies [4–6].
Geometric Epitope and Paratope Prediction
2023, bioRxivGeometric Epitope and Paratope Prediction
2023, arXivStructural mechanism of Fab domain dissociation as a measure of interface stability
2023, Journal of Computer-Aided Molecular Design
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Present address: Teijin Institute for Bio-Medical Research, Teijin Limited, 4-3-2 Asahigaoka, Hino, Tokyo 191, Japan
Copyright © 1993 Published by Elsevier Ltd.