ArticleProtein science : a publication of the Protein Society2019
Application of the NZ-1 Fab as a crystallization chaperone for PA tag-inserted target proteins.
Article in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Preparing for successful protein crystallization experiments.Acta crystallographica. Section F, Structural biology communications · 2025Article
- Cryo-EM structure of the bacterial intramembrane metalloprotease RseP in the substrate-bound state.Science advances · 2025Article
- EMab-300 Detects Mouse Epidermal Growth Factor Receptor-Expressing Cancer Cell Lines in Flow Cytometry.Antibodies (Basel, Switzerland) · 2023Article
- A Novel Anti-CD44 Variant 3 Monoclonal Antibody CInternational journal of molecular sciences · 2023Article
- Development of a Novel Anti-CD44 Variant 5 Monoclonal Antibody CAntibodies (Basel, Switzerland) · 2023Article
- A Novel Anti-CD44 Variant 9 Monoclonal Antibody CCurrent issues in molecular biology · 2023Article
- Development of a Novel Anti-CD44 Variant 7/8 Monoclonal Antibody, CBiomedicines · 2023Article
- Development of a Novel Anti-CD44 Variant 4 Monoclonal Antibody CCurrent issues in molecular biology · 2023Article
- Development of a Novel Anti-CD44 Variant 6 Monoclonal Antibody CInternational journal of molecular sciences · 2023Article
- Development of a Novel Anti-CD44 Monoclonal Antibody for Multiple Applications against Esophageal Squamous Cell Carcinomas.International journal of molecular sciences · 2022Article
- Review
- Structural basis of an epitope tagging system derived from Haloarcula marismortui bacteriorhodopsin I D94N and its monoclonal antibody GD-26.The FEBS journal · 2022Article
- Moving toward generalizable NZ-1 labeling for 3D structure determination with optimized epitope-tag insertion.Acta crystallographica. Section D, Structural biology · 2021Article
- Site-specific epitope insertion into recombinant proteins using the MAP tag system.Journal of biochemistry · 2020Article
- Engineering the Fab fragment of the anti-IgE omalizumab to prevent Fab crystallization and permit IgE-Fc complex crystallization.Acta crystallographica. Section F, Structural biology communications · 2020Article
Corrections and comments
- Erratum issued
Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
An antibody fragment that recognizes the tertiary structure of a target protein with high affinity can be utilized as a crystallization chaperone. Difficulties in establishing conformation-specific antibodies, however, limit the applicability of antibody fragment-assisted crystallization. Here, we attempted to establish an alternative method to promote the crystallization of target proteins using an already established anti-tag antibody. The monoclonal antibody NZ-1 recognizes the PA tag with an extremely high affinity. It was also established that the PA tag is accommodated in the antigen-binding pocket in a bent conformation, compatible with an insertion into loop regions on the target. We, therefore, explored the application of NZ-1 Fab as a crystallization chaperone that complexes with a target protein displaying a PA tag. Specifically, we inserted the PA tag into the β-hairpins of the PDZ tandem fragment of a bacterial Site-2 protease. We crystallized the PA-inserted PDZ tandem mutants with the NZ-1 Fab and solved the co-crystal structure to analyze their interaction modes. Although the initial insertion designs produced only moderate-resolution structures, eliminating the solvent-accessible space between the NZ-1 Fab and target PDZ tandem improved the diffraction qualities remarkably. Our results demonstrate that the NZ-1-PA system efficiently promotes crystallization of the target protein. The present work also suggests that β-hairpins are suitable sites for the PA insertion because the PA tag contains a Pro-Gly sequence with a propensity for a β-turn conformation.
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