The DOI matches its Crossref record; 45 of the 45 references it cites were found in a registry or an index.
Structure of a Complete Integrin Ectodomain in a Physiologic Resting State and Activation and Deactivation by Applied Forces
Open accessAbstract
The complete ectodomain of integrin αIIbβ3 reveals a bent, closed, low-affinity conformation, the β-knee, and a mechanism for linking cytoskeleton attachment to high affinity for ligand. Ca and Mg ions in the recognition site, including the synergistic metal ion binding site (SyMBS), are loaded prior to ligand binding. Electrophilicity of the ligand-binding Mg ion is increased in the open conformation. The β3 knee passes between the β3-PSI and αIIb-knob to bury the lower β-leg in a cleft, from which it is released for extension. Different integrin molecules in crystals and EM reveal breathing that appears on pathway to extension. Tensile force applied to the extended ligand-receptor complex stabilizes the closed, low-affinity conformation. By contrast, an additional lateral force applied to the β subunit to mimic attachment to moving actin filaments stabilizes the open, high-affinity conformation. This mechanism propagates allostery over long distances and couples cytoskeleton attachment of integrins to their high affinity state.
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Scalable molecular dynamics with NAMD
Phillips, J. C., Braun, R., Wang, W., Gumbart, J., Tajkhorshid, E., Villa, E., Chipot, C., Skeel, R. D., Kalé, L., & Schulten, K. (2005) · Journal of Computational Chemistry · doi:10.1002/jcc.20289 · Cited by 16,914
MolProbity: all-atom contacts and structure validation for proteins and nucleic acids
Davis, I. W., Leaver-Fay, A., Chen, V. B., Block, J. N., Kapral, G. J., Wang, X., Murray, L. W., Arendall, W. B., Snoeyink, J., Richardson, J. S., et al. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm216 · Cited by 3,896
Krissinel, E., & Henrick, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904026460 · Cited by 3,760
SPIDER and WEB: Processing and Visualization of Images in 3D Electron Microscopy and Related Fields
Frank, J., Radermacher, M., Penczek, P., Zhu, J., Li, Y., Ladjadj, M., & Leith, A. (1996) · Journal of Structural Biology · doi:10.1006/jsbi.1996.0030 · Cited by 2,027
Self-citationMarlin, S. D., & Springer, T. A. (1987) · Cell · doi:10.1016/0092-8674(87)90104-8 · Cited by 1,674
Self-citationStructural Basis of Integrin Regulation and Signaling
Luo, B.-H., Carman, C. V., & Springer, T. A. (2007) · Annual Review of Immunology · doi:10.1146/annurev.immunol.25.022106.141618 · Cited by 1,660
Self-citationXiong, J.-P., Stehle, T., Zhang, R., Joachimiak, A., Frech, M., Goodman, S. L., & Arnaout, M. A. (2002) · Science · doi:10.1126/science.1069040 · Cited by 1,613
Crystal Structure of the Extracellular Segment of Integrin αVβ3
Xiong, J.-P., Stehle, T., Diefenbach, B., Zhang, R., Dunker, R., Scott, D. L., Joachimiak, A., Goodman, S. L., & Arnaout, M. A. (2001) · Science · doi:10.1126/science.1064535 · Cited by 1,276
Takagi, J., Petre, B. M., Walz, T., & Springer, T. A. (2002) · Cell · doi:10.1016/s0092-8674(02)00935-2 · Cited by 1,168
Self-citationSynergistic Roles for Receptor Occupancy and Aggregation in Integrin Transmembrane Function
Miyamoto, S., Akiyama, S. K., & Yamada, K. M. (1995) · Science · doi:10.1126/science.7846531 · Cited by 888
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Metadata
- Authors
- Zhu, J., Luo, B.-H., Xiao, T., Zhang, C., Nishida, N., & Springer, T. A.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2008-12
- Volume
- 32
- Issue
- 6
- Pages
- 849-861
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2141643986
- Cited by
- 503
- References
- 45
- FWCI
- 20.46
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Zhu, J., Luo, B.-H., Xiao, T., Zhang, C., Nishida, N., & Springer, T. A. (2008). Structure of a Complete Integrin Ectodomain in a Physiologic Resting State and Activation and Deactivation by Applied Forces. Molecular Cell. https://doi.org/10.1016/j.molcel.2008.11.018
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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