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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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Crystal structure of the extracellular segment of integrin alphavbeta3
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Structure:
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Integrin, alpha v. Chain: a. Fragment: residues 31-987. Synonym: vitronectin receptor, alpha polypeptide, antigen cd51. Engineered: yes. Platelet membrane glycoprotein iiia beta subunit. Chain: b. Fragment: residues 27-718. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_taxid: 7108
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Biol. unit:
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Tetramer (from
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Resolution:
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3.10Å
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R-factor:
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0.255
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R-free:
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0.335
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Authors:
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J.P.Xiong,T.Stehle,B.Diefenbach,R.Zhang,R.Dunker,D.Scott, A.Joachimiak,S.L.Goodman,M.A.Arnaout
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Key ref:
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J.P.Xiong
et al.
(2001).
Crystal structure of the extracellular segment of integrin alpha Vbeta3.
Science,
294,
339-345.
PubMed id:
DOI:
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Date:
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28-Aug-01
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Release date:
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17-Oct-01
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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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Science
294:339-345
(2001)
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PubMed id:
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Crystal structure of the extracellular segment of integrin alpha Vbeta3.
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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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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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Selected figure(s)
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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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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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Chem Commun (Camb),
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PDB code:
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H.Xie,
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N.J.Anthis,
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Molecular dynamics simulations of forced unbending of integrin α(v)β₃.
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Ancient origin of the integrin-mediated adhesion and signaling machinery.
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Proc Natl Acad Sci U S A,
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J Biomed Biotechnol,
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C.Rosano,
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Solution properties of full-length integrin alpha(IIb)beta3 refined models suggest environment-dependent induction of alternative bent /extended resting states.
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Structure of the measles virus hemagglutinin bound to the CD46 receptor.
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PDB code:
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C.Selhuber-Unkel,
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Cell adhesion strength is controlled by intermolecular spacing of adhesion receptors.
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A unique interaction between alphaIIb and beta3 in the head region is essential for outside-in signaling-related functions of alphaIIbbeta3 integrin.
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|
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PDB codes:
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M.E.Call,
and
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A view into the blind spot: solution NMR provides new insights into signal transduction across the lipid bilayer.
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N.J.Anthis,
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D.R.Critchley,
and
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|
| |
Structure,
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J Biol Chem,
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J Mol Biol,
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Cardiol Clin,
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Rationally designed integrin beta3 mutants stabilized in the high affinity conformation.
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J Biol Chem,
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C.Faye,
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Biochim Biophys Acta,
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D.Provasi,
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Targeted molecular dynamics reveals overall common conformational changes upon hybrid domain swing-out in beta3 integrins.
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PDB code:
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| |
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|
| |
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A.McDowall,
J.Porter,
and
P.Stanley
(2002).
Mechanisms contributing to the activity of integrins on leukocytes.
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| |
Immunol Rev,
186,
164-171.
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O.Vinogradova,
A.Velyvis,
A.Velyviene,
B.Hu,
T.Haas,
E.Plow,
and
J.Qin
(2002).
A structural mechanism of integrin alpha(IIb)beta(3) "inside-out" activation as regulated by its cytoplasmic face.
|
| |
Cell,
110,
587-597.
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|
PDB code:
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R.C.Liddington,
and
M.H.Ginsberg
(2002).
Integrin activation takes shape.
|
| |
J Cell Biol,
158,
833-839.
|
|
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|
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|
|
R.L.Wilder
(2002).
Integrin alpha V beta 3 as a target for treatment of rheumatoid arthritis and related rheumatic diseases.
|
| |
Ann Rheum Dis,
61,
ii96-ii99.
|
|
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|
R.W.Pickersgill
(2002).
Complex cell signaling molecules from ancient molecular glue.
|
| |
Structure,
10,
1287-1288.
|
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|
|
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S.Fong,
M.V.Doyle,
R.J.Goodson,
R.J.Drummond,
J.R.Stratton,
L.McGuire,
L.V.Doyle,
H.A.Chapman,
and
S.Rosenberg
(2002).
Random peptide bacteriophage display as a probe for urokinase receptor ligands.
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| |
Biol Chem,
383,
149-158.
|
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T.Jackson,
A.P.Mould,
D.Sheppard,
and
A.M.King
(2002).
Integrin alphavbeta1 is a receptor for foot-and-mouth disease virus.
|
| |
J Virol,
76,
935-941.
|
|
|
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|
T.N.Sims,
and
M.L.Dustin
(2002).
The immunological synapse: integrins take the stage.
|
| |
Immunol Rev,
186,
100-117.
|
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Z.Jawad,
and
M.Paoli
(2002).
Novel sequences propel familiar folds.
|
| |
Structure,
10,
447-454.
|
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|
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|
|
T.Kamata,
and
Y.Takada
(2001).
Platelet integrin alphaIIbbeta3-ligand interactions: what can we learn from the structure?
|
| |
Int J Hematol,
74,
382-389.
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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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Links
