The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
INTEGRIN STRUCTURE, ALLOSTERY, AND BIDIRECTIONAL SIGNALING
Abstract
αβ heterodimeric integrins mediate dynamic adhesive cell-cell and cell-extracellular matrix (ECM) interactions in metazoa that are critical in growth and development, hemostasis, and host defense. A central feature of these receptors is their capacity to change rapidly and reversibly their adhesive functions by modulating their ligand-binding affinity. This is normally achieved through interactions of the short cytoplasmic integrin tails with intracellular proteins, which trigger restructuring of the ligand-binding site through long-range conformational changes in the ectodomain. Ligand binding in turn elicits conformational changes that are transmitted back to the cell to regulate diverse responses. The publication of the integrin αVβ3 crystal structure has provided the context for interpreting decades-old biochemical studies. Newer NMR, crystallographic, and EM data, reviewed here, are providing a better picture of the dynamic integrin structure and the allosteric changes that guide its diverse functions.
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Luo, B.-H., Strokovich, K., Walz, T., Springer, T. A., & Takagi, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404354200 · Cited by 73
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Metadata
- Authors
- Arnaout, M. A., Mahalingam, B., & Xiong, J.-P.
- Venue
- Annual Review of Cell and Developmental Biology
- Publisher
- Annual Reviews
- Published
- 2005-11-01
- Volume
- 21
- Issue
- 1
- Pages
- 381-410
- ISSN
- 1081-0706 (ISSN-L)
- 1530-8995
- OpenAlex
- W2154378559
- Cited by
- 550
- References
- 1
- FWCI
- 1.86
- Type
- journal article
- Language
- en
- Open access
- closed
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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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