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* Residue conservation analysis
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PDB id:
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Hormone/growth factor
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Title:
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Crystal structure of bone morphogenetic protein-7 (bmp-7) in with the secreted antagonist noggin
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Structure:
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Bone morphogenetic protein-7. Chain: l. Synonym: bmp-7, osteogenic protein 1, op-1. Engineered: yes. Noggin. Chain: a. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: bmp7. Expressed in: cricetulus griseus. Expression_system_taxid: 10029. Expression_system_cell: ovary cells. Other_details: dhfr-. Gene: nog.
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Biol. unit:
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Tetramer (from PDB file)
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Resolution:
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2.42Å
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R-factor:
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0.242
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R-free:
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0.273
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Authors:
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J.Groppe,J.Greenwald,E.Wiater,J.Rodriguez-Leon,A.N.Economide W.Kwiatkowski,M.Affolter,W.W.Vale,J.C.Izpisua-Belmonte,S.Ch
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Key ref:
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J.Groppe
et al.
(2002).
Structural basis of BMP signalling inhibition by the cystine knot protein Noggin.
Nature,
420,
636-642.
PubMed id:
DOI:
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Date:
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03-Jul-02
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Release date:
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18-Dec-02
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PROCHECK
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Headers
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References
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Gene Ontology (GO) functional annotation
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Cellular component
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extracellular region
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2 terms
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Biological process
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fibroblast growth factor receptor signaling pathway involved in neural plate anterior/posterior pattern formation
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60 terms
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Biochemical function
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cytokine binding
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4 terms
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DOI no:
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Nature
420:636-642
(2002)
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PubMed id:
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Structural basis of BMP signalling inhibition by the cystine knot protein Noggin.
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J.Groppe,
J.Greenwald,
E.Wiater,
J.Rodriguez-Leon,
A.N.Economides,
W.Kwiatkowski,
M.Affolter,
W.W.Vale,
J.C.Belmonte,
S.Choe.
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ABSTRACT
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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. 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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Selected figure(s)
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Figure 2.
Figure 2: Structure of the Noggin -BMP-7 complex. a, Ribbon
diagram of the Noggin -BMP-7 complex in stereo, viewed with the
two-fold symmetry axis vertical. Noggin subunits are blue and
light blue, BMP-7 homodimer subunits are red and gold, sulphur
atoms of cystine linkages are yellow spheres, and the
N-acetylglucosamines of BMP-7 are shown as balls-and-sticks. The
fingers (f1 and f2) of Noggin and BMP-7 are labelled near their
tips. b, Superposition of free (grey) and Noggin-bound (red)
BMP-7 monomers, viewed from above the complex shown in a down
the two-fold axis. c, Noggin -BMP-7 complex coloured as a
rainbow gradient with respect to B-factor values (blue, lowest;
red, highest) to depict relative order and disorder.
Substitutions in disease-causing Noggin mutants are black,
substitutions in variant constructs are light grey (Asp 39, Leu
46, Glu 48, Val 186, Arg 206, Ile 218, Cys 232) or black (Pro
35). Heparin-binding site residues of Noggin (Gln 131 to Lys 144
and putatively Gln 110, Arg 111) are blue. Asn 62 and Thr 64
comprise the N-linked glycosylation signal. Only one set of
residues is labelled, although both chains are marked. Boxed
regions I and II frame the views in Fig. 4b, c, respectively.
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Figure 3.
Figure 3: The Noggin monomer contains a 'growth factor' cystine
knot scaffold. Superposition of Noggin (blue) and free BMP-7
(gold) monomers. Common  -strands
( 1
- 4)
for fingers f1 and f2 are labelled. In the conserved cystine
knot scaffold, 67 C  atoms
align with an r.m.s. deviation of 1.74 Å, which is in the range
(1.4 -3.7 Å) observed for the cystine knot growth factor
superfamily25.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2002,
420,
636-642)
copyright 2002.
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Figures were
selected
by the author.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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Effects of bone morphogenic protein 4 (BMP4) and its inhibitor, Noggin, on in vitro maturation and culture of bovine preimplantation embryos.
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Reprod Biol Endocrinol, 9,
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Efficient targeted gene disruption in the soma and germ line of the frog Xenopus tropicalis using engineered zinc-finger nucleases.
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Biochem J, 429,
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J Tissue Eng Regen Med, 4,
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PDB code:
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J.Nickel,
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X.L.Wu,
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Cross-talk between fibroblast growth factor and bone morphogenetic proteins regulates gap junction-mediated intercellular communication in lens cells.
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PDB code:
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J Biol Chem, 283,
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PDB code:
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T.Kawakami,
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| |
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| |
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Exp Neurol, 204,
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|
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|
| |
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PDB code:
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PDB code:
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J Biol Chem, 279,
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PDB code:
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M.I.Reinhold,
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PDB codes:
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S.Sudo,
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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|
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