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PDBsum entry 1jv2
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Cell adhesion
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PDB id
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1jv2
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the extracellular segment of integrin alpha vbeta3.
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Authors
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J.P.Xiong,
T.Stehle,
B.Diefenbach,
R.Zhang,
R.Dunker,
D.L.Scott,
A.Joachimiak,
S.L.Goodman,
M.A.Arnaout.
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Ref.
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Science, 2001,
294,
339-345.
[DOI no: ]
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PubMed id
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Abstract
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Integrins are alphabeta heterodimeric receptors that mediate divalent
cation-dependent cell-cell and cell-matrix adhesion through tightly regulated
interactions with ligands. We have solved the crystal structure of the
extracellular portion of integrin alphaVbeta3 at 3.1 A resolution. Its 12
domains assemble into an ovoid "head" and two "tails." In
the crystal, alphaVbeta3 is severely bent at a defined region in its tails,
reflecting an unusual flexibility that may be linked to integrin regulation. The
main inter-subunit interface lies within the head, between a seven-bladed
beta-propeller from alphaV and an A domain from beta3, and bears a striking
resemblance to the Galpha/Gbeta interface in G proteins. A metal ion-dependent
adhesion site (MIDAS) in the betaA domain is positioned to participate in a
ligand-binding interface formed of loops from the propeller and betaA domains.
MIDAS lies adjacent to a calcium-binding site with a potential regulatory
function.
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Figure 4.
Fig. 4. (left). Architecture of integrin and G protein
interfaces. The nucleotidebinding folds are in green, and the
propellers are in gray. The integrin is shown in (A) and (B) and
the G protein in (C) and (D). The helices at the core of each
interface are indicated. Integrin's Arg261 and G protein's
Lys210 project toward the respective propeller's central cavity.
G  (Ala^30-Leu348)
and G  (Ser2-Asn340)
are shown. G protein coordinates were from (33).
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Figure 5.
Fig. 5. (right). Surface representation, done with GRASP (42),
of the main V 3 interface
in the head region. Contacting residues (distance cutoff 3.5
Å for hydrogen bonds and salt bridges, and 4.0 Å for
van der Waals contacts) are shown. Arg261 is in blue.
Hydrophobic, ionic, and mixed contacts are in yellow, red, and
orange, respectively. The 3 strands
and helices contributing to the interface are indicated.
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The above figures are
reprinted
by permission from the AAAs:
Science
(2001,
294,
339-345)
copyright 2001.
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