ArticleBMC molecular and cell biology2019
High resolution crystal structure of the FAK FERM domain reveals new insights on the Druggability of tyrosine 397 and the Src SH3 binding site.
Article in BMC molecular and cell biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 21 citations in OpenAlex.
- Discovery of Focal Adhesion Kinase (FAK) activators to promote intestinal mucosal healing.European journal of medicinal chemistry · 2026Article
- Androsin alleviates colorectal cancer by inhibiting the PI3K/Akt-centered signaling pathway.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2026Article
- Recent advances in focal adhesion kinase (FAK)-targeting antitumor agents.RSC advances · 2025Review
- Focal adhesion kinase promotes ribosome biogenesis to drive advanced thyroid cancer cell growth and survival.Frontiers in oncology · 2025Article
- Focal adhesion kinase signaling - tumor vulnerabilities and clinical opportunities.Journal of cell science · 2024Review
- Molecularly imprinted nanoparticles reveal regulatory scaffolding features in Pyk2 tyrosine kinase.RSC chemical biology · 2024Article
- FERM domains recruit ample PI(4,5)PBiophysical journal · 2023Article
- Integrative Ligand-Based Pharmacophore Modeling, Virtual Screening, and Molecular Docking Simulation Approaches Identified Potential Lead Compounds against Pancreatic Cancer by Targeting FAK1.Pharmaceuticals (Basel, Switzerland) · 2023Article
- In Silico Methods for Identification of Potential Active Sites of Therapeutic Targets.Molecules (Basel, Switzerland) · 2022Review
- Computational-based discovery of FAK FERM domain chemical probes that inhibit HER2-FAK cancer signaling.Chemical biology & drug design · 2020Article
- FAK Structure and Regulation by Membrane Interactions and Force in Focal Adhesions.Biomolecules · 2020Review
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
backgroundFocal Adhesion Kinase (FAK) is a major cancer drug target that is involved in numerous aspects of tumor progression and survival. While multiple research groups have developed ATP-competitive small molecule inhibitors that target the kinase enzyme, recent attention has been focused on the FAK FERM (Band 4.1, Ezrin, Radixin, Moesin) domain that contains key residue Y397 and contributes to many protein-protein interactions. Previous x-ray crystal structures of the FAK FERM domain gave conflicting results on the structure of the Y397 region and therefore the overall druggability.
resultsHere, we report the identification of a higher resolution crystal structure of the avian FAK FERM domain that shows conformational differences in Y397 and surrounding residues in the F1 lobe. In addition, we resolve the residues of the Src SH3 binding site, an area of the FERM domain that has previously shown limited electron density.
conclusionsThese crystallographic data suggest that the Y397 region is highly dynamic and question the druggability of a putative pocket on the F1 lobe. In addition, new electron density data around the Src SH3 binding site provide structural insight on the FAK-Src activation cascade through a putative auto-inhibitory conformation.
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