OspA: Difference between revisions
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Here, a 3-D prototype was created to portray its structures. OspA is composed of a prolonged fold with 21 anti-parallel beta sheets and a single alpha helix. They are arranged to form the N-terminal, central sheet and C –terminal barrel domains OspA has numerous features, including a unique folding pattern that includes alternating charge arrays into antiparallel β-sheet, a potential ligand binding site, a conserved surface overlapping the epitope of the Fab, and a distinctive variable motif. It suggests that the protein has a conserved function, possibly acting as a receptor or signal transducer ("Crystal Structure 2012). Although OspA normally has a lipidated N-terminal cysteine to provide a membrane anchor (Brandt 1990), a recombinant unlipidated form is soluble in aqueous solution and is still recognized by antibodies from Lyme disease patients (Dunn 1990). It was identified that three loops of connecting beta strands are the primary sites of binding. | Here, a 3-D prototype was created to portray its structures. OspA is composed of a prolonged fold with 21 anti-parallel beta sheets and a single alpha helix. They are arranged to form the N-terminal, central sheet and C –terminal barrel domains OspA has numerous features, including a unique folding pattern that includes alternating charge arrays into antiparallel β-sheet, a potential ligand binding site, a conserved surface overlapping the epitope of the Fab, and a distinctive variable motif. It suggests that the protein has a conserved function, possibly acting as a receptor or signal transducer ("Crystal Structure 2012). Although OspA normally has a lipidated N-terminal cysteine to provide a membrane anchor (Brandt 1990), a recombinant unlipidated form is soluble in aqueous solution and is still recognized by antibodies from Lyme disease patients (Dunn 1990). It was identified that three loops of connecting beta strands are the primary sites of binding. | ||
<scene name='User:Ji_Youn_Park/Loop_1_52/2'>Loop 1</scene> colored red on the 3-D prototype, consists of residues 203 to 220. However, a natural variation found on <scene name='User:Ji_Youn_Park/Res208_51/ | |||
<scene name='User:Ji_Youn_Park/Loop_1_52/2'>Loop 1</scene> colored red on the 3-D prototype, consists of residues 203 to 220. However, a natural variation found on <scene name='User:Ji_Youn_Park/Res208_51/2'>residue 208</scene> colored yellow, of the first loop is a significant limiting factor in the antibody binding. <scene name='User:Ji_Youn_Park/Loop_2_51/2'>Loop 2</scene>, colored purple, consists of residues 224 to 233. And <scene name='User:Ji_Youn_Park/Loop_3_51/2'>Loop 3</scene> colored blue, consists of residues 246 to 257. The remainder of the beta sheets was colored cyan because they did not play any significant role in OspA. This prototype suggests the importance of the three specific loops and their purpose to binding. | |||