The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Crystal Structure of the Extracellular Segment of Integrin αVβ3
Open accessAbstract
Integrins are αβ 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 αVβ3 at 3.1 Å resolution. Its 12 domains assemble into an ovoid “head” and two “tails.” In the crystal, αVβ3 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 β-propeller from αV and an A domain from β3, and bears a striking resemblance to the Gα/Gβ interface in G proteins. A metal ion–dependent adhesion site (MIDAS) in the βA domain is positioned to participate in a ligand-binding interface formed of loops from the propeller and βA domains. MIDAS lies adjacent to a calcium-binding site with a potential regulatory function.
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Citations
Cites
Protein Structure Comparison by Alignment of Distance Matrices
Holm, L., & Sander, C. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1489 · Cited by 3,984
Cited by
Hynes (2002) · doi:10.1016/s0092-8674(02)00971-6 · Cited by 8,606
Targeting integrin pathways: mechanisms and advances in therapy
Pang, X., He, X., Qiu, Z., Zhang, H., Xie, R., Liu, Z., Gu, Y., Zhao, N., Xiang, Q., & Cui, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01259-6 · Cited by 1,275
The final steps of integrin activation: the end game
Shattil, S. J., Kim, C., & Ginsberg, M. H. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2871 · Cited by 1,086
Photosensitizers with Aggregation‐Induced Emission: Materials and Biomedical Applications
Hu, F., Xu, S., & Liu, B. (2018) · Advanced Materials · doi:10.1002/adma.201801350 · Cited by 859
Bidirectional Transmembrane Signaling by Cytoplasmic Domain Separation in Integrins
Kim, M., Carman, C. V., & Springer, T. A. (2003) · Science · doi:10.1126/science.1084174 · Cited by 786
Metadata
- Authors
- Xiong, J.-P., Stehle, T., Diefenbach, B., Zhang, R., Dunker, R., Scott, D. L., Joachimiak, A., Goodman, S. L., & Arnaout, M. A.
- Venue
- Science
- Published
- 2001-10-12
- Volume
- 294
- Issue
- 5541
- Pages
- 339-345
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1938388466
- Cited by
- 1,276
- References
- 1
- FWCI
- 36.93
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
