Evidence map›Paper›PMID 29273204›Full record

ArticleJournal of molecular biology2018

Locking the Elbow: Improved Antibody Fab Fragments as Chaperones for Structure Determination.

Lucas J Bailey, Kimberly M Sheehy, Pawel K Dominik, Wenguang G Liang, Huan Rui, Michael Clark, Mateusz Jaskolowski, Yejoon Kim, Dawid Deneka, Wei-Jen Tang and 1 more

Abstract read
In one paragraph

Article in Journal of molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

59 citing papers in PubMed.

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  3. Conformational ensembles of the magnesium channel CorA reveal structural basis for channel gating.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  9. Conformational regulation of two essential activators of bacterial cell elongation.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  12. Generation of actionable, cancer-specific neoantigens from KRAS(G12C) with adagrasib.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  13. Conformation-specific synthetic intrabodies modulate mTOR signaling with subcellular spatial resolution.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  18. Structural basis of disease mutation and substrate recognition by the human SLC2A9 transporter.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  19. Engineered protein G variants for multifunctional antibody-based assemblies.Protein science : a publication of the Protein Society · 2025
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  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors.

Lucas J BaileyDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637, USA.
Kimberly M SheehyDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637, USA.
Pawel K DominikDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637, USA.
Wenguang G LiangBen May Institute for Cancer Research, University of Chicago, Chicago, IL 60637, USA.
Huan RuiDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637, USA.
Michael ClarkDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637, USA.
Mateusz JaskolowskiDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637, USA; University of Gdansk and Medical University of Gdansk, International Faculty of Biotechnology, Gdansk, Poland.
Yejoon KimDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637, USA.
Dawid DenekaDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637, USA; Jagiellonian University, Faculty of Biochemistry, Biophysics and Biotechnology, Krakow, Poland.
Wei-Jen TangBen May Institute for Cancer Research, University of Chicago, Chicago, IL 60637, USA.
Anthony A KossiakoffDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637, USA; Institute for Biophysical Dynamics, University of Chicago, Chicago, IL 60637, USA. Electronic address: Koss@bsd.uchicago.edu.

Funding

X-ray Cryst. CoreP50GM082545 · NIGMS · UNIVERSITY OF UTAH · PI SUNDQUIST, WESLEY I. · 2007 to 2018
$51.1M
Synthetic Antigen Binder CoreU54GM087519 · NIGMS · UNIVERSITY OF CHICAGO · PI NAKAMOTO, ROBERT K. · 2010 to 2017
$31.9M
Foreign - Univ. of Toronto, PI-Dr. Sachdev SidhuU01GM094588 · NIGMS · UNIVERSITY OF CHICAGO · PI KOSSIAKOFF, ANTHONY A · 2010 to 2014
$6.8M
Chaperone-Assisted Structure Determination of Membrane ProteinsR01GM117372 · NIGMS · UNIVERSITY OF CHICAGO · PI ANTHONY A KOSSIAKOFF · 2016 to 2026
$4.0M
Regulation and Catalysis of Human Insulin Degrading EnzymeR01GM081539 · NIGMS · UNIVERSITY OF CHICAGO · PI TANG, WEI-JEN · 2007 to 2015
$2.6M
NIGMS NIH HHS P50 GM082545NIGMS NIH HHS R01 GM081539NIGMS NIH HHS R01 GM117372NIGMS NIH HHS U01 GM094588NIGMS NIH HHS U54 GM087519
6 · The paper itself

Abstract

Antibody Fab fragments have been exploited with significant success to facilitate the structure determination of challenging macromolecules as crystallization chaperones and as molecular fiducial marks for single particle cryo-electron microscopy approaches. However, the inherent flexibility of the "elbow" regions, which link the constant and variable domains of the Fab, can introduce disorder and thus diminish their effectiveness. We have developed a phage display engineering strategy to generate synthetic Fab variants that significantly reduces elbow flexibility, while maintaining their high affinity and stability. This strategy was validated using previously recalcitrant Fab-antigen complexes where introduction of an engineered elbow region enhanced crystallization and diffraction resolution. Furthermore, incorporation of the mutations appears to be generally portable to other synthetic antibodies and may serve as a universal strategy to enhance the success rates of Fabs as structure determination chaperones.

Indexed as

AntigensCell Cycle ProteinsCryoelectron MicroscopyCrystallizationHumansImmunoglobulin Fab FragmentsModels, MolecularMolecular ChaperonesPeptide LibraryProtein ConformationProtein EngineeringSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAntigensASF1 protein, S cerevisiaeCell Cycle ProteinsImmunoglobulin Fab FragmentsMolecular ChaperonesPeptide LibrarySaccharomyces cerevisiae Proteinsantibody engineeringcryo-EM fiducial markcrystallization chaperoneFab elbow angleFab–protein complex

Identifiers

PMID29273204
PMCPMC5800945

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.