User:Marvin O'Neal/OspA: Difference between revisions

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     <li><scene name='Studio:G2SecL03/Ospafab-orig/3' target="complex">Reset model</scene><br><br></li>
     <li><scene name='Studio:G2SecL03/Ospafab-orig/3' target="complex">Reset model</scene><br><br></li>
     <li><scene name='Studio:G2SecL03/Ospafab-fab/3' target="complex">LA-2</scene> Fab antibody (Bluish regions indicate heavy chains (chains B & D of 1FJ1) and greenish regions indicate light chains (chains A & C of 1FJ1)</li>
     <li><scene name='Studio:G2SecL03/Ospafab-fab/3' target="complex">LA-2</scene> Fab antibody (Bluish regions indicate heavy chains (chains B & D of 1FJ1) and greenish regions indicate light chains (chains A & C of 1FJ1)</li>
     <li><scene name='Studio:G2SecL03/Ospafab-ospa/3' target="complex">OspA</scene> proteins in complex with the LA-2 Fab antibody</li>
     <li><scene name='Studio:G2SecL03/Ospafab-ospa/3' target="complex">OspA</scene> proteins in complex with the LA-2 Fab antibody (chains E & F of 1FJ1)</li>
     <li><scene name='Studio:G2SecL03/Ospafab-interaction/3' target="complex">Closeup</scene> of the antigen:antibody interactions</li>
     <li><scene name='Studio:G2SecL03/Ospafab-interaction/3' target="complex">Closeup</scene> of the OspA antigen : LA-2 Fab antibody interactions</li>
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OspA is made up of 273 residues over 21 anti-parallel β-sheets and a single α-helix. It's folded conformation is divided into three main sections: a N-terminus "sandwich," a central region comprising of several β-sheets and a C-terminus "barrel" domain.<ref name="ding">PMID: 11183781</ref> The folded regions at its ends are connected by a single β-sheet layer in the middle, giving the protein the unique shape of a dumbell.<ref name="makabe">PMID: 16823038</ref>  
OspA is made up of 273 residues over 21 anti-parallel β-sheets and a single α-helix. It's folded conformation is divided into three main sections: a N-terminus "sandwich," a central region comprising of several β-sheets and a C-terminus "barrel" domain.<ref name="ding">PMID: 11183781</ref> The folded regions at its ends are connected by a single β-sheet layer in the middle, giving the protein the unique shape of a dumbell.<ref name="makabe">PMID: 16823038</ref>  


There are <scene name='Studio:G2SecL03/Ospa-3loops/4' target="OspA-manip">three loops</scene> at the C-terminus of OspA that are important in binding with the LA-2 Fab antibody, whose interactions provide great insight into vaccine research and effectiveness. Within these loops, there are <scene name='Studio:G2SecL03/Ospa-3residues-nor/3' target="OspA-manip">three residues</scene> <scene name='Studio:G2SecL03/Ospa-3residues-r/2' target="OspA-manip">(show residue R-groups)</scene> where there are distinct variations between the different strains of <i>Borrelia</i> and serve as potential targets for the creation of a broader vaccine.<ref name="ding">PMID: 11183781</ref> <scene name='Studio:G2SecL03/Ospa-3loops3res/1' target="OspA-manip">(display both the three loops and three residues together)</scene>  
There are <scene name='Studio:G2SecL03/Ospa-3loops/4' target="OspA-manip">three loops</scene> at the C-terminus of OspA that are important in binding with the LA-2 Fab antibody, whose interactions provide great insight into vaccine research and effectiveness. These three loops are linearly arranged and form protruding ridge at the C-terminus of OspA. Within these loops, there are <scene name='Studio:G2SecL03/Ospa-3residues-nor/3' target="OspA-manip">three residues</scene> <scene name='Studio:G2SecL03/Ospa-3residues-r/2' target="OspA-manip">(show residue R-groups)</scene> where there are distinct variations between the different strains of <i>Borrelia</i> and serve as potential targets for the creation of a broader vaccine.<ref name="ding">PMID: 11183781</ref> <scene name='Studio:G2SecL03/Ospa-3loops3res/1' target="OspA-manip">(display both the three loops and three residues together)</scene>  
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