Evidence map›Paper›PMID 29309709›Full record

ArticleNucleic acids research2018

Affinity maturation of a portable Fab-RNA module for chaperone-assisted RNA crystallography.

Deepak Koirala, Sandip A Shelke, Marcel Dupont, Stormy Ruiz, Saurja DasGupta, Lucas J Bailey, Steven A Benner, Joseph A Piccirilli

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
0.8field-weighted citation impact, top 28% of its field
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

25 citing papers in PubMed, 33 citations in OpenAlex.

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  8. Structure of saguaro cactus virus 3' translational enhancer mimics 5' cap for eIF4E binding.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  15. Discovery of small molecules that target a tertiary-structured RNA.Proceedings of the National Academy of Sciences of the United States of America · 2022
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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

8 authors at 2 institutions in 1 country.

Deepak KoiralaDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL 60637, USA.
Sandip A ShelkeDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL 60637, USA.
Marcel DupontDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL 60637, USA.
Stormy RuizDepartment of Chemistry, The University of Chicago, Chicago, IL 60637, USA.
Saurja DasGuptaDepartment of Chemistry, The University of Chicago, Chicago, IL 60637, USA.
Lucas J BaileyDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL 60637, USA.
Steven A BennerFoundation for Applied Molecular Evolution, Firebird Biomolecular Sciences LLC, 13709 Progress Boulevard, Alachua, FL 32615, USA.
Joseph A PiccirilliDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL 60637, USA.
University of Chicago · USFirebird Biomolecular Sciences (United States) · US

Funding

CHAPERONE-ASSISTED RNA CRYSTALLOGRAPHY - Resubmission 01R01GM102489 · NIGMS · UNIVERSITY OF CHICAGO · PI PICCIRILLI, JOSEPH ANTHONY · 2013 to 2021
$2.9M
Investigating the Catalytic Mechanism of the HDV RibozymeR01AI081987 · NIAID · UNIVERSITY OF CHICAGO · PI PICCIRILLI, JOSEPH ANTHONY · 2010 to 2014
$1.8M
NIAID NIH HHS R01 AI081987NIGMS NIH HHS R01 GM102489
6 · The paper itself

Abstract

Antibody fragments such as Fabs possess properties that can enhance protein and RNA crystallization and therefore can facilitate macromolecular structure determination. In particular, Fab BL3-6 binds to an AAACA RNA pentaloop closed by a GC pair with ∼100 nM affinity. The Fab and hairpin have served as a portable module for RNA crystallization. The potential for general application make it desirable to adjust the properties of this crystallization module in a manner that facilitates its use for RNA structure determination, such as ease of purification, surface entropy or binding affinity. In this work, we used both in vitro RNA selection and phage display selection to alter the epitope and paratope sides of the binding interface, respectively, for improved binding affinity. We identified a 5'-GNGACCC-3' consensus motif in the RNA and S97N mutation in complimentarity determining region L3 of the Fab that independently impart about an order of magnitude improvement in affinity, resulting from new hydrogen bonding interactions. Using a model RNA, these modifications facilitated crystallization under a wider range of conditions and improved diffraction. The improved features of the Fab-RNA module may facilitate its use as an affinity tag for RNA purification and imaging and as a chaperone for RNA crystallography.

Indexed as

Crystallography, X-RayComplementarity Determining RegionsEpitopesImmunoglobulin Fab FragmentsModels, MolecularMutationNucleotide MotifsRNAComplementarity Determining RegionsEpitopesImmunoglobulin Fab FragmentsRNA

Identifiers

PMID29309709
PMCPMC5861428
OpenAlexW2782249869

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.