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* Residue conservation analysis
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DOI no:
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Science
297:1176-1179
(2002)
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PubMed id:
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Structures of glycoprotein Ibalpha and its complex with von Willebrand factor A1 domain.
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E.G.Huizinga,
S.Tsuji,
R.A.Romijn,
M.E.Schiphorst,
P.G.de Groot,
J.J.Sixma,
P.Gros.
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ABSTRACT
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Transient interactions of platelet-receptor glycoprotein Ibalpha (GpIbalpha) and
the plasma protein von Willebrand factor (VWF) reduce platelet velocity at sites
of vascular damage and play a role in haemostasis and thrombosis. Here we
present structures of the GpIbalpha amino-terminal domain and its complex with
the VWF domain A1. In the complex, GpIbalpha wraps around one side of A1,
providing two contact areas bridged by an area of solvated charge interaction.
The structures explain the effects of gain-of-function mutations related to
bleeding disorders and provide a model for shear-induced activation. These
detailed insights into the initial interactions in platelet adhesion are
relevant to the development of antithrombotic drugs.
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Selected figure(s)
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Figure 2.
Fig. 2. Stereo representation of structural changes at the
NH[2]- and COOH-terminal side of VWF-A1. The bottom face of the
A1 domain, as observed in the complex with GpIb  , is shown
in space-filling representation with the NH[2]- and
COOH-terminal peptides shown as C -traces in
yellow. The position of the  finger of
GpIb is given
by a C -trace in
green. The C -traces of
the NH[2]- and COOH-terminal peptides of the uncomplexed,
wild-type (wt) A1 domain (7) are shown in red. Residues with
known gain-of-function mutations yielding a type 2B von
Willebrand disease phenotype are shown either in ball-and-stick
representation in the wt NH[2]- or COOH-terminal peptides or
colored blue in the space-filling model of the bottom face. In
full-length VWF, flanking peptides of A1 possibly shield the
binding site of the finger of
GpIb .
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Figure 3.
Fig. 3. Electrostatic surface potentials of the A1 domain of
VWF and GpIb .
Potentials were calculated for the individual molecules. The
surface is colored blue for potentials > 6 kT/e and red for
potentials <-6 kT/e. The C -traces of
the partner molecules in the complex are shown in white for
clarity. The areas of large electrostatic potentials at the
interface of A1 and GpIb coincide
with the region of loose, solvent-mediated contacts between the
two molecules. Calculations were performed with GRASP (30).
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The above figures are
reprinted
by permission from the AAAs:
Science
(2002,
297,
1176-1179)
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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T.C.White-Adams,
M.A.Berny,
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R.T.Urbanus,
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Platelet activation by dimeric beta2-glycoprotein I requires signaling via both glycoprotein Ibalpha and apolipoprotein E receptor 2'.
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J Thromb Haemost,
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S.Z.Luo,
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Specific heteromeric association of four transmembrane peptides derived from platelet glycoprotein Ib-IX complex.
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(2008).
Platelet glycoprotein Ibalpha forms catch bonds with human WT vWF but not with type 2B von Willebrand disease vWF.
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J Clin Invest,
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PDB code:
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PDB code:
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PDB code:
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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
codes are
shown on the right.
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