Unique epitope–antibody interactions in the intrinsically disordered proteoglycan-like domain of human carbonic anhydrase IX defined by high-resolution NMR combined with yeast surface display

Unique epitope–antibody interactions in the intrinsically disordered proteoglycan-like domain of human carbonic anhydrase IX defined by high-resolution NMR combined with yeast surface display

ABSTRACTCarbonic anhydrase (CA)-IX is an extracellular enzyme that is essential in the adaptation of tumor cells to their increasingly more hypoxic and acidic microenvironment. Within the family of carbonic anhydrases, CA-IX is unique in that it is the only CA with an N-terminal intrinsically disord...

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Bibliographic Details
Main Authors: Feng Ni, Cunle Wu, Ping Xu, Ping Wang, Yves Fortin, Melanie Arbour, Luke Masson, Denis L’Abbé, Andrea Acel, Mylene Gosselin, Anne E.G. Lenferink
Format: Article
Language:English
Published: Taylor & Francis Group 2023-12-01
Series:mAbs
Subjects:
Antibodies
antibody–antigen interactions
carbonic anhydrase IX
epitope mapping
F(ab)
intrinsically disordered proteins
Online Access:https://www.tandfonline.com/doi/10.1080/19420862.2023.2248672

Internet

https://www.tandfonline.com/doi/10.1080/19420862.2023.2248672

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