BMP6 binding to heparin and heparan sulfate is mediated by N-terminal and C-terminal clustered basic residues

• Published in: Biochimica et biophysica acta. General subjects Vol. 1865; no. 2; p. 129799
• Main Authors: Denardo, Andrea, Elli, Stefano, Federici, Stefania, Asperti, Michela, Gryzik, Magdalena, Ruzzenenti, Paola, Carmona, Fernando, Bergese, Paolo, Naggi, Annamaria, Arosio, Paolo, Poli, Maura
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.02.2021
• Subjects: Animals; Binding Sites; Bone morphogenetic protein 6 (BMP6); Bone Morphogenetic Protein 6 - chemistry; Bone Morphogenetic Protein 6 - metabolism; bone morphogenetic proteins; CHO Cells; computer simulation; Cricetulus; Hep G2 Cells; Heparan sulfate; Heparin; Heparin - metabolism; Heparitin Sulfate - metabolism; Hepcidin; Hepcidins - metabolism; Humans; Interaction; Models, Molecular; mutation; Protein Binding; Protein Interaction Domains and Motifs; sulfates; Heparan sulfate; HSPG; Interaction; Bone morphogenetic protein 6 (BMP6); HS; HBD; GAG; BMP6; DS; CS; MD; Heparin; SEC-TDA; Hepcidin

The bone morphogenetic protein 6 (BMP6) is a crucial inducer of hepcidin, the peptide hormone that regulates the iron availability in our body. Hepcidin expression is influenced by hepatic heparan sulfate (HS) and by heparin administration, suggesting BMP6 interaction with heparin/HS. The BMP2/4 sub...