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The Arg-Gly-Asp binding domain of the vitronectin receptor. Photoaffinity cross-linking implicates amino acid residues 61-203 of the beta subunit.
Open accessAbstract
We have employed photoaffinity cross-linking to examine RGD recognition by the human placental vitronectin receptor. The peptide GRGDSPK was coupled to a thiol-cleavable radioiodinatable aryl azide (sulfosuccinimidyl 2-(p-azido-salicylamido)-1,3'-dithiopropionate. When 125I-sulfosuccinimidyl 2-(p-azido-salicylamido)-1,3'-dithiopropionate-GRGDSPK was cross-linked to the vitronectin receptor in solution, 80% of the label was associated with the beta subunit. Cross-linking to both subunits of the receptor was highly specific and dependent upon the presence of divalent cations. Ca2+ and Mg2+ promoted RGD recognition by the receptor; however, the effects of each divalent cation were kinetically distinct. We have also identified and determined the amino acid sequence of chymotryptic and V8 protease-generated peptides of the beta subunit that were radiolabeled as a result of cross-linking. The results of these studies demonstrate that amino acid residues 61-203 are proximal to the RGD binding domain of the vitronectin receptor.
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Cited by
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Ratner, B. D., & Bryant, S. J. (2004) · Annual Review of Biomedical Engineering · doi:10.1146/annurev.bioeng.6.040803.140027 · Cited by 1,507
Extracellular Matrix Molecules And Their Receptors: Functions In Neural Development
Reichardt, L. F., & Tomaselli, K. J. (1991) · Annual Review of Neuroscience · doi:10.1146/annurev.ne.14.030191.002531 · Cited by 750
Diamond, M. S., Garcia-Aguilar, J., Bickford, J. K., Corbi, A. L., & Springer, T. A. (1993) · The Journal of cell biology · doi:10.1083/jcb.120.4.1031 · Cited by 533
Xu, J., Rodriguez, D., Petitclerc, E., Kim, J. J., Hangai, M., Yuen, S. M., Davis, G. E., & Brooks, P. C. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200103111 · Cited by 489
Metadata
- Authors
- Smith, J. W., & Cheresh, D. A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1988-12
- Volume
- 263
- Issue
- 35
- Pages
- 18726-18731
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1594881395
- Cited by
- 234
- References
- 0
- FWCI
- 7.60
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: The Arg-Gly-Asp binding domain of the vitronectin receptor. Photoaffinity cross-linking implicates amino acid residues 61-203 of the beta subunit. https://app.cochat.ai/papers/10.1016/s0021-9258(18)37343-5
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- Smith, J. W., & Cheresh, D. A. (1988). The Arg-Gly-Asp binding domain of the vitronectin receptor. Photoaffinity cross-linking implicates amino acid residues 61-203 of the beta subunit. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)37343-5
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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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