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Crystal Structure of the Extracellular Segment of Integrin V3
Jian-Ping Xiong,1Thilo Stehle,12Beate Diefenbach,3Rongguang Zhang,4Reinhardt Dunker,3David L. Scott,1Andrzej Joachimiak,4Simon L. Goodman,3M. Amin Arnaout1*
Integrins are heterodimeric receptors that mediate
divalent cation-dependent cell-cell and cell-matrix adhesion throughtightly regulated interactions with ligands. We have solved thecrystal
structure of the extracellular portion of integrin V3at 3.1 Å resolution. Its 12 domains assemble into an ovoid "head"and two
"tails." In the crystal, V3 is severely bent at a definedregion in its tails, reflecting an unusual flexibility that maybe
linked to integrin regulation. The main inter-subunit interfacelies
within the head, between a seven-bladed -propeller fromV and an
A domain from 3, and bears a striking resemblance tothe G/G
interface in G proteins. A metal ion-dependent adhesionsite (MIDAS)
in the A domain is positioned to participate ina ligand-binding
interface formed of loops from the propellerand A domains. MIDAS
lies adjacent to a calcium-binding sitewith a potential regulatory
function.
1 Renal Unit, Leukocyte Biology & Inflammation
Program, Structural Biology Program, Massachusetts General Hospital and
Harvard Medical School, 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 Departments of
Biotechnology and Biomedical Research Immunology/Oncology, Merck KGaA,
Darmstadt 64271, Germany.
4 Biosciences Division,
Argonne National Laboratory, IL 60439, USA
*
To whom correspondence should be addressed. E-mail:
arnaout{at}receptor.mgh.harvard.edu
The editors suggest the following Related Resources on Science sites:
In Science Magazine
PERSPECTIVES
Martin J. Humphries and A. Paul Mould (12 October 2001) Science294 (5541), 316.
[DOI: 10.1126/science.1066240] |Summary »|Full Text »|PDF »
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|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 »
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 »
Integrin Activation State Determines Selectivity for Novel Recognition Sites in Fibrillar Collagens.
P. R.-M. Siljander, S. Hamaia, A. R. Peachey, D. A. Slatter, P. A. Smethurst, W. H. Ouwehand, C. G. Knight, and R. W. Farndale (2004)
J. Biol. Chem.
279, 47763-47772
|Abstract »|Full Text »|PDF »
The integrin {alpha}-subunit leg extends at a Ca2+-dependent epitope in the thigh/genu interface upon activation.
C. Xie, M. Shimaoka, T. Xiao, P. Schwab, L. B. Klickstein, and T. A. Springer (2004)
PNAS
101, 15422-15427
|Abstract »|Full Text »|PDF »
A Novel Adaptation of the Integrin PSI Domain Revealed from Its Crystal Structure.
J.-P. Xiong, T. Stehle, S. L. Goodman, and M. A. Arnaout (2004)
J. Biol. Chem.
279, 40252-40254
|Abstract »|Full Text »|PDF »
Interactions of Foot-and-Mouth Disease Virus with Soluble Bovine {alpha}V{beta}3 and {alpha}V{beta}6 Integrins.
H. Duque, M. LaRocco, W. T. Golde, and B. Baxt (2004)
J. Virol.
78, 9773-9781
|Abstract »|Full Text »|PDF »
Integrins: dynamic scaffolds for adhesion and signaling in platelets.
Inaugural Article: Integrin {beta}3 regions controlling binding of murine mAb 7E3: Implications for the mechanism of integrin {alpha}IIb{beta}3 activation.
A. Artoni, J. Li, B. Mitchell, J. Ruan, J. Takagi, T. A. Springer, D. L. French, and B. S. Coller (2004)
PNAS
101, 13114-13120
|Abstract »|Full Text »|PDF »
V
3
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 
