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* Residue conservation analysis
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PDB id:
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Cell adhesion
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Title:
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Structural basis for allostery in integrins and binding of ligand- mimetic therapeutics to the platelet receptor for fibrinogen
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Structure:
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Integrin alpha-iib. Chain: a, c, e. Fragment: residues 1-452. Synonym: platelet membrane glycoprotein iib. Gpalpha iib. Gpiib. Cd41 antigen. Engineered: yes. Integrin beta-3. Chain: b, d, f. Fragment: residues 1-440.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: itgab. Expressed in: cricetulus griseus. Expression_system_taxid: 10029. Expression_system_cell: hampster ovary cells.
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Biol. unit:
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Dimer (from
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Resolution:
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2.90Å
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R-factor:
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0.219
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R-free:
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0.254
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Authors:
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T.Xiao,J.Takagi,B.S.Coller,J.-H.Wang,T.A.Springer
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Key ref:
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T.Xiao
et al.
(2004).
Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics.
Nature,
432,
59-67.
PubMed id:
DOI:
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Date:
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07-Jul-04
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Release date:
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12-Oct-04
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PROCHECK
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Headers
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References
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DOI no:
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Nature
432:59-67
(2004)
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PubMed id:
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Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics.
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T.Xiao,
J.Takagi,
B.S.Coller,
J.H.Wang,
T.A.Springer.
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ABSTRACT
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Integrins are important adhesion receptors in all Metazoa that transmit
conformational change bidirectionally across the membrane. Integrin alpha and
beta subunits form a head and two long legs in the ectodomain and span the
membrane. Here, we define with crystal structures the atomic basis for
allosteric regulation of the conformation and affinity for ligand of the
integrin ectodomain, and how fibrinogen-mimetic therapeutics bind to platelet
integrin alpha(IIb)beta3. Allostery in the beta3 I domain alters three metal
binding sites, associated loops and alpha1- and alpha7-helices. Piston-like
displacement of the alpha7-helix causes a 62 degrees reorientation between the
beta3 I and hybrid domains. Transmission through the rigidly connected
plexin/semaphorin/integrin (PSI) domain in the upper beta3 leg causes a 70 A
separation between the knees of the alpha and beta legs. Allostery in the head
thus disrupts interaction between the legs in a previously described
low-affinity bent integrin conformation, and leg extension positions the
high-affinity head far above the cell surface.
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Selected figure(s)
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Figure 1.
Figure 1: Quaternary rearrangements in the integrin ectodomain.
a -c, Three conformational states visualized in electron
microscopy3,6 and in crystal structures (here and in ref. 7). d
-j, Proposed intermediates in equilibration between known
conformational states. The upper pathways may be stimulated by
ligand binding outside the cell, and the lower pathways by
signals within the cell that separate the  and
 subunit
transmembrane domains. Domains in a -j are shown in solid colour
if known directly from crystal structures, dashed with grey if
placed from crystal structures into electron microscopy image
averages, and in solid grey for EGF-1 and EGF-2, which are
modelled on EGF-3 and EGF-4.
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Figure 3.
Figure 3: The binding sites for ligand-mimetic antagonists and
fibrinogen at the alpha- /
beta- subunit
interface. a, Mapping of fibrinogen binding sensitive
mutations20,49,50 in [IIb]
[3].
C atoms
of fibrinogen-binding sensitive residues are shown as spheres in
the same colour as the domains in which they are present. The
tirofiban-bound structure is shown. b -f, Binding of ligands or
pseudoligands to [IIb]
[3]
(b -e) and binding of (f) cyclo Arg-Gly-Asp-D-Phe-N-methyl-Val
(cyclo RGDfV) to [V]
[3]
(ref. 8). The orientation is identical to that in a. The and
subunits
are shown in magenta and cyan, respectively. Small molecules are
shown as ball-and-stick models with their carbon, nitrogen,
oxygen, sulphur and arsenic atoms coloured yellow, blue, red,
green and grey, respectively. Hydrogen bonds are shown as dotted
lines. Ca^2+ and Mg2+ ions are gold and silver spheres,
respectively. The ligand and S123 coordinations to the MIDAS
metal are shown as thin grey lines.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2004,
432,
59-67)
copyright 2004.
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Figures were
selected
by an automated process.
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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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A.P.Silverman,
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Cystine-knot peptides engineered with specificities for α(IIb)β(3) or α(IIb)β(3) and α(v)β(3) integrins are potent inhibitors of platelet aggregation.
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J Mol Recognit,
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Impact of {beta}2 integrin deficiency on mouse natural killer cell development and function.
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Blood,
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N.J.Anthis,
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EMBO J,
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PDB codes:
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D.Cox,
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and
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The biomechanical integrin.
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J Biomech,
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Structures of C3b in complex with factors B and D give insight into complement convertase formation.
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Science,
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PDB codes:
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H.Hauschner,
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|
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(2010).
Structural basis of semaphorin-plexin recognition and viral mimicry from Sema7A and A39R complexes with PlexinC1.
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Cell,
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749-761.
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PDB codes:
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I.Le Trong,
P.Aprikian,
B.A.Kidd,
M.Forero-Shelton,
V.Tchesnokova,
P.Rajagopal,
V.Rodriguez,
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Cell,
141,
645-655.
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PDB code:
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J.A.Askari,
C.J.Tynan,
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C.Ballestrem,
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Focal adhesions are sites of integrin extension.
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188,
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(2010).
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Closed headpiece of integrin αIIbβ3 and its complex with an αIIbβ3-specific antagonist that does not induce opening.
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Blood,
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PDB codes:
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R.Huang,
I.Martinez-Ferrando,
and
P.A.Cole
(2010).
Enhanced interrogation: emerging strategies for cell signaling inhibition.
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and
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|
| |
J Virol,
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J Mol Biol,
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D.Provasi,
M.Murcia,
B.S.Coller,
and
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(2009).
Targeted molecular dynamics reveals overall common conformational changes upon hybrid domain swing-out in beta3 integrins.
|
| |
Proteins,
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M.Poncz,
and
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(2009).
Quinine-dependent, platelet-reactive monoclonals mimic antibodies found in patients with quinine-induced immune thrombocytopenia.
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Blood,
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(2009).
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J.Qin,
and
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Kindling the flame of integrin activation and function with kindlins.
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K.Sigmundsson,
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L.G.Ofverstedt,
S.Svensson,
U.Skoglund,
and
B.Obrink
(2009).
The CEACAM1 N-terminal Ig domain mediates cis- and trans-binding and is essential for allosteric rearrangements of CEACAM1 microclusters.
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J Cell Biol,
187,
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and
V.Vogel
(2009).
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J Biol Chem,
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A.J.García,
A.P.Mould,
M.J.Humphries,
and
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(2009).
Demonstration of catch bonds between an integrin and its ligand.
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| |
J Cell Biol,
185,
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E.Mortier,
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(2009).
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J Cell Sci,
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PDB code:
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(2009).
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| |
Proc Natl Acad Sci U S A,
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(2009).
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|
| |
Blood,
114,
4883-4885.
|
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PDB code:
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R.B.Basani,
H.Zhu,
M.A.Thornton,
C.S.Soto,
W.F.Degrado,
M.A.Kowalska,
J.S.Bennett,
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M.Poncz
(2009).
Species differences in small molecule binding to alpha IIb beta 3 are the result of sequence differences in 2 loops of the alpha IIb beta propeller.
|
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Blood,
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R.Blue,
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M.Murcia,
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M.Jirouskova,
J.Li,
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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
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