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The Bone morphogenetic protein 4 (BMP4) precursor protein is cleaved at two sites to generate an active ligand and inactive prodomain. The ligand and prodomain form a noncovalent complex following… Click to show full abstract
The Bone morphogenetic protein 4 (BMP4) precursor protein is cleaved at two sites to generate an active ligand and inactive prodomain. The ligand and prodomain form a noncovalent complex following the first cleavage, but dissociate after the second cleavage. Transient formation of this complex is essential to generate a stable ligand. Fibrillins (FBNs) bind to the prodomains of BMPs, and can regulate the activity of some ligands. Whether FBNs regulate BMP4 activity is unknown.
Keywords:
evidence fibrillin1;
lack evidence;
activity;
bone morphogenetic;
morphogenetic protein;
protein
Journal Title: Developmental Dynamics
Year Published: 2023
Link to full text (if available)
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Journal Title: Developmental Dynamics
Year Published: 2023
Link to full text (if available)
Share on Social Media: Sign Up to like & get
recommendations!