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. 2002 Dec 12;420(6916):636-42.
doi: 10.1038/nature01245.

V体育官网 - Structural basis of BMP signalling inhibition by the cystine knot protein Noggin

Jay Groppe  1 , Jason Greenwald, Ezra Wiater, Joaquin Rodriguez-Leon, Aris N Economides, Witek Kwiatkowski, Markus Affolter, Wylie W Vale, Juan Carlos Izpisua Belmonte, Senyon Choe
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"V体育官网入口" Structural basis of BMP signalling inhibition by the cystine knot protein Noggin

"V体育2025版" Jay Groppe et al. Nature. .

Abstract

The interplay between bone morphogenetic proteins (BMPs) and their antagonists governs developmental and cellular processes as diverse as establishment of the embryonic dorsal-ventral axis, induction of neural tissue, formation of joints in the skeletal system and neurogenesis in the adult brain. So far, the three-dimensional structures of BMP antagonists and the structural basis for inactivation have remained unknown. Here we report the crystal structure of the antagonist Noggin bound to BMP-7, which shows that Noggin inhibits BMP signalling by blocking the molecular interfaces of the binding epitopes for both type I and type II receptors VSports手机版. The BMP-7-binding affinity of site-specific variants of Noggin is correlated with alterations in bone formation and apoptosis in chick limb development, showing that Noggin functions by sequestering its ligand in an inactive complex. The scaffold of Noggin contains a cystine (the oxidized form of cysteine) knot topology similar to that of BMPs; thus, ligand and antagonist seem to have evolved from a common ancestral gene. .

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