ArticleJournal of molecular biology2015
Structure of Full-Length Human PDGFRβ Bound to Its Activating Ligand PDGF-B as Determined by Negative-Stain Electron Microscopy.
Article in Journal of molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 53 citations in OpenAlex.
- Growth factor applications and clinical translation: advances and challenges.Annals of medicine · 2026Review
- The Molecular Neurobiology of NG2-Expressing Glial Cells in Cerebral Small Vessel Disease Pathogenesis.Molecular neurobiology · 2026Review
- Applying Computational Protein Design to Engineer Affibodies for Affinity-controlled Delivery of Vascular Endothelial Growth Factor and Platelet-Derived Growth Factor.Biomacromolecules · 2025Article
- Reanalysis of cryo-EM data reveals ALK-cytokine assemblies with both 2:1 and 2:2 stoichiometries.PLoS biology · 2025Article
- Single-molecule imaging and molecular dynamics simulations reveal early activation of the MET receptor in cells.Nature communications · 2024Article
- Receptor Tyrosine Kinase: Still an Interesting Target to Inhibit the Proliferation of Vascular Smooth Muscle Cells.American journal of cardiovascular drugs : drugs, devices, and other interventions · 2023Review
- Cryo-EM analyses of KIT and oncogenic mutants reveal structural oncogenic plasticity and a target for therapeutic intervention.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- PDGFR dimer-specific activation, trafficking and downstream signaling dynamics.Journal of cell science · 2022Article
- Okicamelliaside targets the N-terminal chaperone pocket of HSP90 disrupts the chaperone protein interaction of HSP90-CDC37 and exerts antitumor activity.Acta pharmacologica Sinica · 2022Article
- An effective strategy for ligand-mediated pulldown of the HER2/HER3/NRG1β heterocomplex and cryo-EM structure determination at low sample concentrations.Methods in enzymology · 2022Article
- Efficient expression, purification, and visualization by cryo-EM of unliganded near full-length HER3.Methods in enzymology · 2022Article
- Article
- Engineering and crystal structure of a monomeric FLT3 ligand variant.Acta crystallographica. Section F, Structural biology communications · 2021Article
- PDGF receptor mutations in human diseases.Cellular and molecular life sciences : CMLS · 2021Review
- The emerging complexity of PDGFRs: activation, internalization and signal attenuation.Biochemical Society transactions · 2020Review
- Engineered receptors for human cytomegalovirus that are orthogonal to normal human biology.PLoS pathogens · 2020Article
- Receptor tyrosine kinase activation: From the ligand perspective.Current opinion in cell biology · 2020Review
- Role of Platelet-Derived Growth Factor (PDGF) in Asthma as an Immunoregulatory Factor Mediating Airway Remodeling and Possible Pharmacological Target.Frontiers in pharmacology · 2020Review
- A Detailed Protocol for Large-scale Recombinant Expression and Validation of Human FGFR2 with Its Transmembrane and Extracellular Domains inBio-protocol · 2019Article
- More than the sum of the parts: Toward full-length receptor tyrosine kinase structures.IUBMB life · 2019Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Members of the receptor tyrosine kinases (RTKs) regulate important cellular functions such as cell growth and migration, which are key steps in angiogenesis, in organ morphogenesis and in the unregulated states, cancer formation. One long-standing puzzle regarding RTKs centers on how the extracellular domain (ECD), which detects and binds to growth factors, is coupled with the intracellular domain kinase activation. While extensive structural works on the soluble portions of RTKs have provided critical insights into RTK structures and functions, lack of a full-length receptor structure has hindered a comprehensive overview of RTK activation. In this study, we successfully purified and determined a 27-Å-resolution structure of PDGFRβ [a full-length human platelet-derived growth factor receptor], in complex with its ligand PDGF-B. In the ligand-stimulated complex, two PDGFRβs assemble into a dimer via an extensive interface essentially running along the full-length of the receptor, suggesting that the membrane-proximal region, the transmembrane helix and the kinase domain of PDGFRβ are involved in dimerization. Major structural differences are seen between the full-length and soluble ECD structures, rationalizing previous experimental data on how membrane-proximal domains modulate receptor ligand-binding affinity and dimerization efficiency. Also, in contrast to the 2-fold symmetry of the ECD, the intracellular kinase domains adopt an asymmetric dimer arrangement, in agreement with prior observations for the closely related KIT receptor. In essence, the structure provides a first glimpse into how platelet-derived growth factor receptor ECD, upon ligand stimulation, is coupled to its intracellular domain kinase activation.
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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.