Evidence map›Paper›PMID 39046952›Full record

ArticlePLoS computational biology2024

A comprehensive exploration of the druggable conformational space of protein kinases using AI-predicted structures.

Noah B Herrington, Yan Chak Li, David Stein, Gaurav Pandey, Avner Schlessinger

Abstract read
In one paragraph

Article in PLoS computational biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

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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

10 citing papers in PubMed.

  1. Article
  2. Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Noah B HerringtonDepartment of Pharmacological Sciences, Icahn School of Medicine at Mount Sinai, New York, New York, United States of America.ORCID 0000-0002-9467-238X
Yan Chak LiDepartment of Genetics and Genomic Sciences, Icahn School of Medicine at Mount Sinai, New York, New York, United States of America.
David SteinDepartment of Pharmacological Sciences, Icahn School of Medicine at Mount Sinai, New York, New York, United States of America.
Gaurav PandeyDepartment of Genetics and Genomic Sciences, Icahn School of Medicine at Mount Sinai, New York, New York, United States of America.ORCID 0000-0003-1939-679X
Avner SchlessingerDepartment of Pharmacological Sciences, Icahn School of Medicine at Mount Sinai, New York, New York, United States of America.ORCID 0000-0003-4007-7814

Funding

Conduits: Mount Sinai Health System Translational Science HubUL1TR004419 · NCATS · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI Rosalind J Wright · 2022 to 2026
$46.4M
Multi-modal data integration to identify kinase substratesU01CA271318 · NCI · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI PANDEY, GAURAV, SCHLESSINGER, AVNER · 2022 to 2023
$1.0M
NCATS NIH HHS UL1 TR004419NCI NIH HHS U01 CA271318
6 · The paper itself

Abstract

Protein kinase function and interactions with drugs are controlled in part by the movement of the DFG and ɑC-Helix motifs that are related to the catalytic activity of the kinase. Small molecule ligands elicit therapeutic effects with distinct selectivity profiles and residence times that often depend on the active or inactive kinase conformation(s) they bind. Modern AI-based structural modeling methods have the potential to expand upon the limited availability of experimentally determined kinase structures in inactive states. Here, we first explored the conformational space of kinases in the PDB and models generated by AlphaFold2 (AF2) and ESMFold, two prominent AI-based protein structure prediction methods. Our investigation of AF2's ability to explore the conformational diversity of the kinome at various multiple sequence alignment (MSA) depths showed a bias within the predicted structures of kinases in DFG-in conformations, particularly those controlled by the DFG motif, based on their overabundance in the PDB. We demonstrate that predicting kinase structures using AF2 at lower MSA depths explored these alternative conformations more extensively, including identifying previously unobserved conformations for 398 kinases. Ligand enrichment analyses for 23 kinases showed that, on average, docked models distinguished between active molecules and decoys better than random (average AUC (avgAUC) of 64.58), but select models perform well (e.g., avgAUCs for PTK2 and JAK2 were 79.28 and 80.16, respectively). Further analysis explained the ligand enrichment discrepancy between low- and high-performing kinase models as binding site occlusions that would preclude docking. The overall results of our analyses suggested that, although AF2 explored previously uncharted regions of the kinase conformational space and select models exhibited enrichment scores suitable for rational drug discovery, rigorous refinement of AF2 models is likely still necessary for drug discovery campaigns.

Indexed as

Computational BiologyProtein ConformationProtein KinasesDatabases, ProteinHumansLigandsModels, MolecularProtein Kinase InhibitorsSequence AlignmentLigandsProtein Kinase InhibitorsProtein Kinases

Identifiers

PMID39046952
PMCPMC11268620

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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.