Pertactin sandbox1: Difference between revisions

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==Structure and Protein Adhesion Properties==

[[Image:autotransporter.jpg]]

Pertactin is a single unit protein consisting of a 16-stranded parallel beta-helix with a v-shaped cross section. There are two conserved domains within Pertactin, an autotransporter domain located at the N-terminus and a passenger domain located at the C-terminus (“Conserved,” 2015). Pathogens such as Bordetella pertussis and Bordetella parapertussis utilize virulence factors to adhere to target cells, which contribute to the overall pathogenicity of the organism. Pertactin shares homology with other proteins that are known to aid in cell-cell adhesion, emphasizing the importance of structure and how it relates to function. P.69 pertactin has been shown to adhere to mammalian cells, and has several features that contribute to this functionality (Emsley et al., 1996). One of these features is the Arg-Gly-Asp (RGD) tripeptide motif that allows for protein-protein interactions (Emsley et al., 1996). 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 (D’Souza, Ginsberg, & Plow, 1991). Additionally, P.69 contains two proline-rich regions, which are thought to provide important binding sites, and are characteristic of proteins exhibiting binding capabilities (Emsley et al., 1996). 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 (Williamson, 1994). 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 (Emsley et al., 1996). 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 (Gallant, Michael, & Garcia, 2005).

== Function==

Pertactin sandbox1: Difference between revisions

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@@ Line 10: / Line 10: @@
 ==Structure and Protein Adhesion Properties==
 [[Image:autotransporter.jpg]]
+Pertactin is a single unit protein consisting of a 16-stranded parallel beta-helix with a v-shaped cross section.  There are two conserved domains within Pertactin, an autotransporter domain located at the N-terminus and a passenger domain located at the C-terminus (“Conserved,” 2015). Pathogens such as Bordetella pertussis and Bordetella parapertussis utilize virulence factors to adhere to target cells, which contribute to the overall pathogenicity of the organism. Pertactin shares homology with other proteins that are known to aid in cell-cell adhesion, emphasizing the importance of structure and how it relates to function. P.69 pertactin has been shown to adhere to mammalian cells, and has several features that contribute to this functionality (Emsley et al., 1996). One of these features is the Arg-Gly-Asp (RGD) tripeptide motif that allows for protein-protein interactions (Emsley et al., 1996). 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 (D’Souza, Ginsberg, & Plow, 1991). Additionally, P.69 contains two proline-rich regions, which are thought to provide important binding sites, and are characteristic of proteins exhibiting binding capabilities (Emsley et al., 1996). 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 (Williamson, 1994). 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 (Emsley et al., 1996). 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 (Gallant, Michael, & Garcia, 2005).
 == Function==