1zkz: Difference between revisions

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[[Image:1zkz.gif|left|200px]]
{{Seed}}
[[Image:1zkz.png|left|200px]]


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{{STRUCTURE_1zkz|  PDB=1zkz  |  SCENE=  }}  
{{STRUCTURE_1zkz|  PDB=1zkz  |  SCENE=  }}  


'''Crystal Structure of BMP9'''
===Crystal Structure of BMP9===




==Overview==
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Bone morphogenetic proteins (BMPs), a subset of the transforming growth factor (TGF)-beta superfamily, regulate a diverse array of cellular functions during development and in the adult. BMP-9 (also known as growth and differentiation factor (GDF)-2) potently induces osteogenesis and chondrogenesis, has been implicated in the differentiation of cholinergic neurons, and may help regulate glucose metabolism. We have determined the structure of BMP-9 to 2.3 A and examined the differences between our model and existing crystal structures of other BMPs, both in isolation and in complex with their receptors. TGF-beta ligands are translated as precursors, with pro-regions that generally dissociate after cleavage from the ligand, but in some cases (including GDF-8 and TGF-beta1, -2, and -3), the pro-region remains associated after secretion from the cell and inhibits binding of the ligand to its receptor. Although the proregion of BMP-9 remains tightly associated after secretion, we find, in several cell-based assays, that the activities of BMP-9 and BMP-9.pro-region complex were equivalent. Activin receptor-like kinase 1 (ALK-1), an orphan receptor in the TGF-beta family, was also identified as a potential receptor for BMP-9 based on surface plasmon resonance studies (BIAcore) and the ability of soluble ALK-1 to block the activity of BMP-9.pro-region complex in cell-based assays.
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{{ABSTRACT_PUBMED_15851468}}


==About this Structure==
==About this Structure==
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[[Category: Growth factor]]
[[Category: Growth factor]]
[[Category: Signal]]
[[Category: Signal]]
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