G09SecL04Tpc2: Difference between revisions

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Albert Kurian, Nabil Faridi, Amar Patole, Michal Harel

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 == Outer Surface Protein A (OspA) ==
-<Structure load='1fj1' size='350' frame='true' align='right' caption='Outer Surface Protein A Fab LA-2 Complex' scene='G09SecL04Tpc2/Startospa/3' />
+<Structure load='1fj1' size='350' frame='true' align='right' caption='Outer Surface Protein A' scene='G09SecL04Tpc2/Startospa/3' />
 <scene name='G09SecL04Tpc2/Startospa/3'>Reset Model</scene>
 === Structural Breakdown ===
-Outer Surface ProteinA has approximately 270 amino acid residues. <ref name=art3>PMID:11183781</ref>In terms of secondary structure, OspA is made up of 21 anti-parallel single layer beta strands and one alpha helix. <ref name=art3>PMID:11183781</ref>OspA has three major components to its structure: an n-terminal sandwich, a central sheet, and a c-terminal barrel domains. The n-terminal is often termed as a sandwich due to its jumbled formation of amino acid residues. Most of the beta strands lie on the central sheet. Lastly, the c-terminal is called barrel domains because the three primary loops connect to both sides of the central beta sheet forming a barrel or a hole in the middle. This can be seen by rotating the molecule.
+Outer Surface Protein A has approximately 270 amino acid residues. <ref name=art3>PMID:11183781</ref>In terms of secondary structure, OspA is made up of 21 anti-parallel single layer beta strands and one alpha helix. <ref name=art3>PMID:11183781</ref>OspA has three major components to its structure: an <scene name='G09SecL04Tpc2/3sites/3'>n-terminal sandwich</scene>, <scene name='G09SecL04Tpc2/3sites/2'>a central sheet</scene>, and a c-terminal barrel domains. The n-terminal is often termed as a sandwich due to its jumbled formation of amino acid residues. Most of the beta strands lie on the central sheet. Lastly, the c-terminal is called barrel domains because the three primary loops connect to both sides of the central beta sheet forming a barrel or a hole in the middle. This can be seen by rotating the molecule.
 The c-terminal is heavily involved in the antigen:antibody complex unlike the n-terminal. The c-terminal houses a protruding ridge of three loops: loop 1 contains residues 203-220; loop 2 contains residues 224-233; loop 3 contains residues 246-257. These loops define the LA-2 (antibody) epitope. More specifically, the loops indicate where the antibody binds to the antigen. This protruding ridge coupled with OspA’s elongated fold gives the surface protein a high degree of mobility and surface exposure.