StudioG24SecL04Tpc5: Difference between revisions
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==Structural Overview== | ==Structural Overview== | ||
The relationship between VlsE structure and its possible functions were determined by the three dimensional structure of VlsE from the [http://en.wikipedia.org/wiki/Borrelia_burgdorferi ''Borrelia burgdorferi''] <br> B31 strain. <ref>PMID: 11923306</ref> VlsE is shown to be composed of four sub-units, each consisting of a variable domain flanked by two invariable domains (Liang). The variable domains themselves contain six <scene name='StudioG24SecL04Tpc5/Variable_region/2'>variable regions</scene> (VR) interspersed amongst six invariable regions (IR). The IRs are embedded deep within the protein covered by alpha helical loops. The IRs are embedded deep within the protein being essentially shielded by the VRs which represent 37% of the total surface area while containing less than 26% of the primary protein sequence. <ref>PMID: 11923306</ref> The six VRs entirely cover the distal portion of the protein with about 50% of their theoretical surface area exposed to the surface for immune response. <ref>PMID: 11923306</ref>. In contrast, the portion of the sub-unit responsible for the antigenic variation in the VlsE as well as inducing the host’s immune response only exposes about 13.7% of its surface. Being shielded by the IRs, the host’s antibodies are restricted to interact with a very limited number of residues rendering any antigenic response futile. | The relationship between VlsE structure and its possible functions were determined by the three dimensional structure of VlsE from the [http://en.wikipedia.org/wiki/Borrelia_burgdorferi ''Borrelia burgdorferi''] <br> B31 strain. <ref>PMID: 11923306</ref> VlsE is shown to be composed of four sub-units, each consisting of a variable domain flanked by two invariable domains (Liang). The variable domains themselves contain six <scene name='StudioG24SecL04Tpc5/Variable_region/2'>variable regions</scene> (VR) interspersed amongst six invariable regions (IR). The IRs are embedded deep within the protein covered by alpha helical loops. The IRs are embedded deep within the protein being essentially shielded by the VRs which represent 37% of the total surface area while containing less than 26% of the primary protein sequence. <ref>PMID: 11923306</ref> The six VRs entirely cover the distal portion of the protein with about 50% of their theoretical surface area exposed to the surface for immune response. <ref>PMID: 11923306</ref>. In contrast, the portion of the sub-unit responsible for the antigenic variation in the VlsE as well as inducing the host’s immune response only exposes about 13.7% of its surface. Being shielded by the IRs, the host’s antibodies are restricted to interact with a very limited number of residues rendering any antigenic response futile. | ||
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===Invariable=== | ===Invariable=== | ||
Invariable Region:<scene name='StudioG24SecL04Tpc5/Invariable_regions/1'>IR</scene> | Invariable Region:<scene name='StudioG24SecL04Tpc5/Invariable_regions/1'>IR</scene> | ||
The small invariable regions within the variable region as well as the larger invariable domains C & N terminals are not antigenic in natural infections and tend to be conserved among different isolates of the organism. Conserved portions are probably responsible for the maintenance of the functional and molecular conformations of the VlsE. They maintain the secondary structure of the protein, the beta sheets and alpha helix. This allows the protein to maintain its functional properties because the alpha and beta sheets allow the secondary structure to be stable enough to allow the side chains of the VlsE protein to construct a biologically active tertiary structure. | The small invariable regions within the variable region as well as the larger invariable domains C & N terminals are not antigenic in natural infections and tend to be conserved among different isolates of the organism. Conserved portions are probably responsible for the maintenance of the functional and molecular conformations of the VlsE. They maintain the secondary structure of the protein, the | ||
[http://public.csusm.edu/jayasinghe/BiomolTutorials/HelicesAndSheets/HelicesAndSheets.html beta sheets and alpha helix]. This allows the protein to maintain its functional properties because the alpha and beta sheets allow the secondary structure to be stable enough to allow the side chains of the VlsE protein to construct a biologically active tertiary structure. | |||