Pertactin sandbox1: Difference between revisions

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Kimberly Eldridge, Melissa Gray, Rachel Korba, Claire Gormley, Zackary Zayakosky

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 One of these features is the Arg-Gly-Asp (RGD) tripeptide motif that allows for protein-protein interactions <ref name="EMS" />. This motif has been found in several proteins, and has been shown to support cell adhesion in most cases. A subset of cell-surface proteins, called integrins, act as receptors for cell adhesion molecules. These integrins recognize the RGD motif within their ligands, and allow for cell-substratum and cell-cell interactions <ref>D'Souza, S. E., Ginsberg, M. H., & Plow, E. F. (1991). Arginyl-glycyl-aspartic acid (RGD): a cell adhesion motif. Trends In Biochemical Sciences, 16(7), 246-250.</ref>.
-Additionally, P.69 contains two proline-rich regions, which are thought to provide important binding sites, and are characteristic of proteins exhibiting binding capabilities <ref name="EMS" />. Proline is a very unusual amino acid, and its structure limits the possible conformations it can adopt. Especially when chains of proline are bound to each other, the rigidity of these structures allow for reliable binding sites in many different proteins. These regions are typically non-specific, and allow for rapid binding. This is advantageous due to the wide range of ligands that can be bound, increasing the versatility of the proteins that utilize these regions <ref>Williamson, M. P. (1994). The structure and function of proline-rich regions in proteins. Biochemical Journal, 297(Pt 2), 249–260.</ref>.
+Additionally, P.69 contains two <scene name='71/716564/Proline/2'>proline-rich regions</scene> which are thought to provide important binding sites, and are characteristic of proteins exhibiting binding capabilities <ref name="EMS" />. Proline is a very unusual amino acid, and its structure limits the possible conformations it can adopt. Especially when chains of proline are bound to each other, the rigidity of these structures allow for reliable binding sites in many different proteins. These regions are typically non-specific, and allow for rapid binding. This is advantageous due to the wide range of ligands that can be bound, increasing the versatility of the proteins that utilize these regions <ref>Williamson, M. P. (1994). The structure and function of proline-rich regions in proteins. Biochemical Journal, 297(Pt 2), 249–260.</ref>.
 The linear form of pertactin that protrudes from the surface of ''B. pertussis'' also has a high surface area that could be well suited for targeting mammalian cells <ref name="EMS" />. Studies have shown that adhesive area strongly affects integrin binding and adhesion strength. The positioning of binding regions also affects adhesion strength, making the combination of these two factors particularly important for proteins that serve this function <ref>Gallant, N. D., Michael, K. E., & García, A. J. (2005). Cell Adhesion Strengthening: Contributions of Adhesive Area, Integrin Binding, and Focal Adhesion Assembly. Molecular Biology of the Cell, 16(9), 4329–4340.</ref>.