Structural basis for the contribution of latent TGFβ binding protein to TGFβ latency and activation.
- Open access
Cryo-EM structure reveals how LTBP1 binding modulates TGFβ latency and activation, highlighting a hydrophobic interface crucial for complex formation and activity.
- Why it matters: Understanding TGFβ regulation is vital because it controls cellular behavior and is involved in many diseases; however, the structural basis of its latency and activation remains unclear.
- What they did: The study used cryo-electron microscopy to determine the LLC structure, showing LTBP1 covalently bound to TGFβ and identifying key interfaces through mutagenesis and simulations.
- The result: Findings demonstrate that LTBP1 influences force distribution within the complex, reducing unfolding barriers and informing potential therapeutic strategies targeting TGFβ activation.