Evidence map›Paper›PMID 41660693›Full record

ArticleActa crystallographica. Section F, Structural biology communications2026

Crystallization and X-ray structure of a highly aggregation-prone monobody engineered for high-affinity small-molecule recognition.

Koushirou Endo, Shun Umemoto, Nariaki Tsuzuki, Hideo Okumura, Yusuke Sato, Tatsuyuki Yoshii, Shinya Tsukiji, Shingo Nagano, Hiroshi Murakami, Tomoya Hino

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

10 authors.

Koushirou EndoDepartment of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University, 4-101 Koyamacho-minami, Tottori, Tottori 680-8552, Japan.
Shun UmemotoDepartment of Biomolecular Engineering, Graduate School of Engineering, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, Aichi 464-8601, Japan.ORCID 0000-0001-6212-9449
Nariaki TsuzukiDepartment of Biomolecular Engineering, Graduate School of Engineering, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, Aichi 464-8601, Japan.
Hideo OkumuraDiffraction and Scattering Division, Japan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5198, Japan.ORCID 0000-0003-1652-4776
Yusuke SatoDepartment of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University, 4-101 Koyamacho-minami, Tottori, Tottori 680-8552, Japan.ORCID 0000-0001-8495-8950
Tatsuyuki YoshiiDepartment of Life Science and Applied Chemistry, Nagoya Institute of Technology, Gokiso-cho, Showa-ku, Nagoya, Aichi 466-8555, Japan.ORCID 0000-0002-3465-4219
Shinya TsukijiDepartment of Life Science and Applied Chemistry, Nagoya Institute of Technology, Gokiso-cho, Showa-ku, Nagoya, Aichi 466-8555, Japan.ORCID 0000-0002-1402-5773
Shingo NaganoDepartment of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University, 4-101 Koyamacho-minami, Tottori, Tottori 680-8552, Japan.ORCID 0000-0002-9292-8759
Hiroshi MurakamiDepartment of Biomolecular Engineering, Graduate School of Engineering, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, Aichi 464-8601, Japan.ORCID 0000-0003-2089-9263
Tomoya HinoDepartment of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University, 4-101 Koyamacho-minami, Tottori, Tottori 680-8552, Japan.ORCID 0000-0002-8813-4622

Funding

Japan Society for the Promotion of Science 23H05456Japan Society for the Promotion of Science JP22H04753
6 · The paper itself

Abstract

Monobodies, engineered protein scaffolds derived from the fibronectin type III domain, are powerful alternatives to conventional antibodies. While the native scaffold is robust, engineering the variable loops can often compromise solubility and promote aggregation. Here, we report the crystallization and structure determination at 2.57 Å resolution of a monobody (Mb-P') engineered to bind the synthetic small molecule HPPU [1-(4-hydroxyphenyl)-3-phenylurea] with nanomolar affinity. Although Mb-P' exhibited severe polydispersity and heterogeneous oligomerization in solution, N-terminal fusion with maltose-binding protein (MBP) using an optimized linker successfully yielded monodisperse species and diffraction-quality crystals. The crystal structure exhibited pseudo-D

Indexed as

Maltose-Binding ProteinsProtein EngineeringRecombinant Fusion ProteinsCrystallizationCrystallography, X-RayProtein AggregatesMaltose-Binding ProteinsProtein AggregatesRecombinant Fusion Proteinsaggregationfusion-protein crystallizationin situ X-ray diffractionmaltose-binding proteinmonobodies

Identifiers

PMID41660693
PMCPMC12961676

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Registered trials

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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.