Evidence map›Paper›PMID 38187589›Full record

ArticlebioRxiv : the preprint server for biology2023

De novo design of diverse small molecule binders and sensors using Shape Complementary Pseudocycles.

Linna An, Meerit Said, Long Tran, Sagardip Majumder, Inna Goreshnik, Gyu Rie Lee, David Juergens, Justas Dauparas, Ivan Anishchenko, Brian Coventry and 15 more

Open access · greenAbstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed, 14 citations in OpenAlex.

  1. Review
  2. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

25 authors at 4 institutions in 3 countries.

Linna AnDepartment of Biochemistry, The University of Washington, Seattle, WA, USA.ORCID 0000-0001-9858-9105
Meerit SaidDepartment of Biochemistry, The University of Washington, Seattle, WA, USA.
Long TranDepartment of Chemical Engineering, University of Washington, Seattle, WA, USA.
Sagardip MajumderDepartment of Biochemistry, The University of Washington, Seattle, WA, USA.
Inna GoreshnikDepartment of Biochemistry, The University of Washington, Seattle, WA, USA.
Gyu Rie LeeDepartment of Biochemistry, The University of Washington, Seattle, WA, USA.
David JuergensDepartment of Biochemistry, The University of Washington, Seattle, WA, USA.
Justas DauparasDepartment of Biochemistry, The University of Washington, Seattle, WA, USA.
Ivan AnishchenkoDepartment of Biochemistry, The University of Washington, Seattle, WA, USA.
Brian CoventryDepartment of Biochemistry, The University of Washington, Seattle, WA, USA.
Asim K BeraDepartment of Biochemistry, The University of Washington, Seattle, WA, USA.
Alex KangDepartment of Biochemistry, The University of Washington, Seattle, WA, USA.
Paul M LevineDepartment of Biochemistry, The University of Washington, Seattle, WA, USA.
Valentina AlvarezDepartment of Biochemistry, The University of Washington, Seattle, WA, USA.
Arvind PillaiDepartment of Biochemistry, The University of Washington, Seattle, WA, USA.
Christoffer NornBioInnovation Institute, DK2200 Copenhagen N, Denmark.
David FeldmanBioInnovation Institute, DK2200 Copenhagen N, Denmark.
Dmitri ZorineDepartment of Biochemistry, The University of Washington, Seattle, WA, USA.
Derrick R HicksDepartment of Biochemistry, The University of Washington, Seattle, WA, USA.
Xinting LiInstitute for Protein Design, University of Washington, Seattle, WA, USA.
Mariana Garcia SanchezInstitute for Protein Design, University of Washington, Seattle, WA, USA.
Dionne K VafeadosInstitute for Protein Design, University of Washington, Seattle, WA, USA.
Patrick J SalvesonDepartment of Biochemistry, The University of Washington, Seattle, WA, USA.
Anastassia A VorobievaVIB-VUB Center for Structural Biology, Belgium.
David BakerDepartment of Biochemistry, The University of Washington, Seattle, WA, USA.
University of Washington · USBioInnovation Institute · DKHoward Hughes Medical Institute · USVIB-VUB Center for Structural Biology · BE

Funding

X-ray Scattering Technology CoreP30GM133893 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI Sean McSweeney · 2019 to 2026
$38.6M
User Training and OutreachP30GM124165 · NIGMS · CORNELL UNIVERSITY · PI Nozomi Ando, J Christopher Fromme · 2018 to 2026
$34.2M
Centers for Research on Structural Biology of Infectious Diseases: Universal Influenza Vaccine Research75N93022C00036 · NIAID · SEATTLE CHILDREN'S HOSPITAL · PI STAKER, BART · 2022 to 2025
$21.7M
Project 4: Novel reagent development to enable molecular characterizationU19AG065156 · NIA · UNIVERSITY OF WASHINGTON · PI MACCOSS, MICHAEL · 2020 to 2024
$15.9M
De Novo Design of Minibinder Antagonists for COVID-19 and Future PandemicsR01AI160052 · NIAID · UNIVERSITY OF WASHINGTON · PI BAKER, DAVID, FULLER, DEBORAH H. · 2021 to 2025
$3.5M
Designed Vehicles for Blood Brain Barrier TraversalR01AG063845 · NIA · UNIVERSITY OF WASHINGTON · PI BAKER, DAVID · 2019 to 2023
$2.5M
NIAID NIH HHS 75N93022C00036NIAID NIH HHS HHSN272201700059CNIAID NIH HHS R01 AI160052NIA NIH HHS R01 AG063845NIA NIH HHS U19 AG065156NIGMS NIH HHS P30 GM124165NIGMS NIH HHS P30 GM133893
6 · The paper itself

Abstract

A general method for designing proteins to bind and sense any small molecule of interest would be widely useful. Due to the small number of atoms to interact with, binding to small molecules with high affinity requires highly shape complementary pockets, and transducing binding events into signals is challenging. Here we describe an integrated deep learning and energy based approach for designing high shape complementarity binders to small molecules that are poised for downstream sensing applications. We employ deep learning generated psuedocycles with repeating structural units surrounding central pockets; depending on the geometry of the structural unit and repeat number, these pockets span wide ranges of sizes and shapes. For a small molecule target of interest, we extensively sample high shape complementarity pseudocycles to generate large numbers of customized potential binding pockets; the ligand binding poses and the interacting interfaces are then optimized for high affinity binding. We computationally design binders to four diverse molecules, including for the first time polar flexible molecules such as methotrexate and thyroxine, which are expressed at high levels and have nanomolar affinities straight out of the computer. Co-crystal structures are nearly identical to the design models. Taking advantage of the modular repeating structure of pseudocycles and central location of the binding pockets, we constructed low noise nanopore sensors and chemically induced dimerization systems by splitting the binders into domains which assemble into the original pseudocycle pocket upon target molecule addition.

Identifiers

PMID38187589
PMCPMC10769206
OpenAlexW4390080474

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

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.