This is the C-terminal domain of Chordin-like proteins 1 and 2 (CHRDL1/2). CHRDL1 antagonizes the function of BMP4 by binding to it and preventing its interaction with receptors []. CHRDL2 inhibit bone morphogenetic proteins (BMPs) activity by blocking their interaction with their receptor []. CHRDL2 may play a role during myoblast and osteoblast differentiation and maturation []. It's worth noting that there are different results regarding its binding partners; according to [], CHRDL2 interacts with INHBA but not BMP2, BMP4 and BMP6.
This entry includes chordin-like protein 1/2 (CHRDL1/2). CHRDL1 antagonizes the function of BMP4 by binding to it and preventing its interaction with receptors []. CHRDL2 inhibit bone morphogenetic proteins (BMPs) activity by blocking their interaction with their receptor []. CHRDL2 may play a role during myoblast and osteoblast differentiation and maturation []. It's worth noting that there are different results regarding its binding partners; according to [], CHRDL2 interacts with INHBA but not BMP2, BMP4 and BMP6.Bone is composed of an organic matrix that is principally collagenous and is mineralised with inorganic crystals of hydroxyapatite. Demineralisation of the bone results in a demineralised bone matrix []. In 1965, Urist M.R demonstrates the decalcified bone matrix (DBM) can induce ectopic bone/cartilage formation []. The morphogens in DBM that induce such skeletogenesis were named as bone morphogenetic proteins (BMPs) []. Since then, more than 20 members of BMPs have been identified. BMPs are potent effectors in almost all crucial biological events, such development, maintenance and regeneration of organs/tissues [].
