[HTML][HTML] Two distinct regions of latency-associated peptide coordinate stability of the latent transforming growth factor-β1 complex
Transforming growth factor-β1 (TGF-β1) is secreted as part of an inactive complex consisting
of the mature dimer, the TGF-β1 propeptide (latency-associated peptide (LAP)), and latent
TGF-β-binding proteins. Using in vitro mutagenesis, we identified the regions of LAP that
govern the cooperative assembly and stability of the latent TGF-β1 complex. Initially,
hydrophobic LAP residues (Ile 53, Leu 54, Leu 57, and Leu 59), which form a contiguous
epitope on one surface of an amphipathic α-helix, interact with mature TGF-β1 to form the …
of the mature dimer, the TGF-β1 propeptide (latency-associated peptide (LAP)), and latent
TGF-β-binding proteins. Using in vitro mutagenesis, we identified the regions of LAP that
govern the cooperative assembly and stability of the latent TGF-β1 complex. Initially,
hydrophobic LAP residues (Ile 53, Leu 54, Leu 57, and Leu 59), which form a contiguous
epitope on one surface of an amphipathic α-helix, interact with mature TGF-β1 to form the …