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Crystal Structure of the Extracellular Segment of Integrin V3 in Complex with an Arg-Gly-Asp Ligand
Jian-Ping Xiong,1Thilo Stehle,12*Rongguang Zhang,3*Andrzej Joachimiak,3Matthias Frech,4Simon L. Goodman,5M. Amin Arnaout1
The structural basis for the divalent
cation-dependent binding of heterodimeric integrins to their
ligands, which containthe prototypical Arg-Gly-Asp sequence, is
unknown. Interactionwith ligands triggers tertiary and quaternary
structural rearrangementsin integrins that are needed for cell
signaling. Here we reportthe crystal structure of the extracellular
segment of integrinV3 in complex with a cyclic peptide
presenting the Arg-Gly-Aspsequence. The ligand binds at the major
interface between theV and 3 subunits and makes extensive
contacts with both. Bothtertiary and quaternary changes are observed
in the presence ofligand. The tertiary rearrangements take place in
A, the ligand-bindingdomain of 3; in the complex, A acquires
two cations, one ofwhich contacts the ligand Asp directly and the
other stabilizesthe ligand-binding surface. Ligand binding induces
small changesin the orientation of V relative to 3.
1 Renal Unit, Leukocyte Biology and
Inflammation Program, Structural Biology Program, Massachusetts General
Hospital, 149 13th Street, Charlestown, MA 02129, USA.
2 Laboratory of Developmental Immunology,
Massachusetts General Hospital, and Harvard Medical School, 55 Fruit
Street, Boston, MA 02114, USA.
3 Argonne National
Laboratory, Biosciences Division, Structural Biology Center, IL 60439, USA.
4 Department of Target Research,
5 Biomedical Research, Oncology, Merck KGaA,
Darmstadt 64271, Germany.
*
These two authors contributed equally to this work.
To whom correspondence should be addressed. E-mail:
arnaout{at}receptor.mgh.harvard.edu
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|Abstract »|Full Text »|PDF »
Synergistic effects of light-emitting probes and peptides for targeting and monitoring integrin expression.
S. Achilefu, S. Bloch, M. A. Markiewicz, T. Zhong, Y. Ye, R. B. Dorshow, B. Chance, and K. Liang (2005)
PNAS
102, 7976-7981
|Abstract »|Full Text »|PDF »
Three-dimensional EM structure of the ectodomain of integrin {alpha}V{beta}3 in a complex with fibronectin.
B. D. Adair, J.-P. Xiong, C. Maddock, S. L. Goodman, M. A. Arnaout, and M. Yeager (2005)
J. Cell Biol.
168, 1109-1118
|Abstract »|Full Text »|PDF »
Dual Functionality of the Anti-{beta}1 Integrin Antibody, 12G10, Exemplifies Agonistic Signalling from the Ligand Binding Pocket of Integrin Adhesion Receptors.
J. D. Humphries, N. R. Schofield, Z. Mostafavi-Pour, L. J. Green, A. N. Garratt, A. P. Mould, and M. J. Humphries (2005)
J. Biol. Chem.
280, 10234-10243
|Abstract »|Full Text »|PDF »
Dual Function for a Unique Site within the {beta}2I Domain of Integrin {alpha}M{beta}2.
D. Ehirchiou, Y.-M. Xiong, Y. Li, S. Brew, and L. Zhang (2005)
J. Biol. Chem.
280, 8324-8331
|Abstract »|Full Text »|PDF »
GSH Inhibits Trypsinization of the C-terminal Half of Human MRP1.
X.-Q. Ren, T. Furukawa, Y. Nakajima, H. Takahashi, S. Aoki, T. Sumizawa, M. Haraguchi, M. Kobayashi, K. Chijiiwa, and S.-i. Akiyama (2005)
J. Biol. Chem.
280, 6231-6237
|Abstract »|Full Text »|PDF »
Evidence That Monoclonal Antibodies Directed against the Integrin {beta} Subunit Plexin/Semaphorin/Integrin Domain Stimulate Function by Inducing Receptor Extension.
A. P. Mould, M. A. Travis, S. J. Barton, J. A. Hamilton, J. A. Askari, S. E. Craig, P. R. MacDonald, R. A. Kammerer, P. A. Buckley, and M. J. Humphries (2005)
J. Biol. Chem.
280, 4238-4246
|Abstract »|Full Text »|PDF »
Design, Synthesis, and Analysis of a Polyethelene Glycol-Modified (PEGylated) Small Molecule Inhibitor of Integrin {alpha}4{beta}1 with Improved Pharmaceutical Properties.
R. B. Pepinsky, W.-C. Lee, M. Cornebise, A. Gill, K. Wortham, L. L. Chen, D. R. Leone, K. Giza, B. M. Dolinski, S. Perper, et al. (2005)
J. Pharmacol. Exp. Ther.
312, 742-750
|Abstract »|Full Text »|PDF »
Pathogenic hantaviruses bind plexin-semaphorin-integrin domains present at the apex of inactive, bent {alpha}v{beta}3 integrin conformers.
T. Raymond, E. Gorbunova, I. N. Gavrilovskaya, and E. R. Mackow (2005)
PNAS
102, 1163-1168
|Abstract »|Full Text »|PDF »
Distinct Roles for the {alpha} and {beta} Subunits in the Functions of Integrin {alpha}M{beta}2.
D. A. Solovjov, E. Pluskota, and E. F. Plow (2005)
J. Biol. Chem.
280, 1336-1345
|Abstract »|Full Text »|PDF »
Imaging of Delayed-Type Hypersensitivity Reaction by PET and 18F-Galacto-RGD.
B. J. Pichler, M. Kneilling, R. Haubner, H. Braumuller, M. Schwaiger, M. Rocken, and W. A. Weber (2005)
J. Nucl. Med.
46, 184-189
|Abstract »|Full Text »|PDF »
The Relative Influence of Metal Ion Binding Sites in the I-like Domain and the Interface with the Hybrid Domain on Rolling and Firm Adhesion by Integrin {alpha}4{beta}7.
J. Chen, J. Takagi, C. Xie, T. Xiao, B.-H. Luo, and T. A. Springer (2004)
J. Biol. Chem.
279, 55556-55561
|Abstract »|Full Text »|PDF »
Interdomain Tilt Angle Determines Integrin-dependent Function of the Ninth and Tenth FIII Domains of Human Fibronectin.
H. Altroff, R. Schlinkert, C. F. van der Walle, A. Bernini, I. D. Campbell, J. M. Werner, and H. J. Mardon (2004)
J. Biol. Chem.
279, 55995-56003
|Abstract »|Full Text »|PDF »
The Integrin {alpha}L{beta}2 Hybrid Domain Serves as a Link for the Propagation of Activation Signal from Its Stalk Regions to the I-like Domain.
E. Tng, S.-M. Tan, S. Ranganathan, M. Cheng, and S. K. A. Law (2004)
J. Biol. Chem.
279, 54334-54339
|Abstract »|Full Text »|PDF »
A 50-A Separation of the Integrin {alpha}v{beta}3 Extracellular Domain C Termini Reveals an Intermediate Activation State.
S. E. Gline, S. Cambier, C. Govaerts, and S. L. Nishimura (2004)
J. Biol. Chem.
279, 54567-54572
|Abstract »|Full Text »|PDF »
Functional and structural correlations of individual {alpha}IIb{beta}3 molecules.
R. I. Litvinov, C. Nagaswami, G. Vilaire, H. Shuman, J. S. Bennett, and J. W. Weisel (2004)
Blood
104, 3979-3985
|Abstract »|Full Text »|PDF »
Combinatorial antibody libraries from cancer patients yield ligand-mimetic Arg-Gly-Asp-containing immunoglobulins that inhibit breast cancer metastasis.
B. Felding-Habermann, R. A. Lerner, A. Lillo, S. Zhuang, M. R. Weber, S. Arrues, C. Gao, S. Mao, A. Saven, and K. D. Janda (2004)
PNAS
101, 17210-17215
|Abstract »|Full Text »|PDF »
V
3 in Complex with an Arg-Gly-Asp Ligand
integrins to their
ligands, which contain the prototypical Arg-Gly-Asp sequence, is
unknown. Interaction with ligands triggers tertiary and quaternary
structural rearrangements in integrins that are needed for cell
signaling. Here we report the crystal structure of the extracellular
segment of integrin 
