Chordin (CHRD (gene symbol); no widely accepted protein abbreviation for the molecule, commonly referred to as "Chordin")

Chordin is a secreted extracellular protein of 941 amino acids with a compact horseshoe-shaped structure, notable for four cysteine-rich von Willebrand factor C (vWC) domains that mediate high-affinity cooperative binding to bone morphogenetic proteins (BMP-2, BMP-4, BMP-7, ADMP)[1][4][2]. By tightly binding BMPs in the extracellular space, chordin blocks their interaction with BMP receptors—thereby inhibiting BMP-mediated ventralizing signaling and promoting dorsal/anterior and neural tissue formation during early vertebrate development. Its activity is regulated by cleavage via tolloid metalloproteinases, which can modulate its inhibition potency and turnover[1]. Chordin interacts with cofactors such as Twisted Gastrulation (Tsg), collagen IV, Crossveinless-2 (CV2), and is homologous to Sog in Drosophila. Mutations in chordin disrupt dorsal-ventral axis formation and neural development in animal models but there is no current evidence for direct relevance to human disease or use as a therapeutic target[4][3][2].

Other names

CHRDChordin (typically used in literature for molecule and gene)"Sog" (homolog in Drosophila)

Not applicable — Chordin is not a therapeutic target of drugs, but acts by binding and sequestering BMPs, preventing their interaction with BMP receptors