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PDBsum entry 2mbk
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Signaling protein
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PDB id
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2mbk
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References listed in PDB file
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Key reference
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Title
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The clip-Segment of the von willebrand domain 1 of the bmp modulator protein crossveinless 2 is preformed.
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Authors
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J.E.Fiebig,
S.E.Weidauer,
L.Y.Qiu,
M.Bauer,
P.Schmieder,
M.Beerbaum,
J.L.Zhang,
H.Oschkinat,
W.Sebald,
T.D.Mueller.
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Ref.
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Molecules, 2013,
18,
11658-11682.
[DOI no: ]
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PubMed id
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Abstract
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Bone Morphogenetic Proteins (BMPs) are secreted protein hormones that act as
morphogens and exert essential roles during embryonic development of tissues and
organs. Signaling by BMPs occurs via hetero-oligomerization of two types of
serine/threonine kinase transmembrane receptors. Due to the small number of
available receptors for a large number of BMP ligands ligand-receptor
promiscuity presents an evident problem requiring additional regulatory
mechanisms for ligand-specific signaling. Such additional regulation is achieved
through a plethora of extracellular antagonists, among them members of the
Chordin superfamily, that modulate BMP signaling activity by binding. The
key-element in Chordin-related antagonists for interacting with BMPs is the von
Willebrand type C (VWC) module, which is a small domain of about 50 to 60
residues occurring in many different proteins. Although a structure of the VWC
domain of the Chordin-member Crossveinless 2 (CV2) bound to BMP-2 has been
determined by X-ray crystallography, the molecular mechanism by which the VWC
domain binds BMPs has remained unclear. Here we present the NMR structure of the
Danio rerio CV2 VWC1 domain in its unbound state showing that the key features
for high affinity binding to BMP-2 is a pre-oriented peptide loop.
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