G09SecL04Tpc2: Difference between revisions
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== Structure == | == Structure == | ||
Outer Surface ProteinA has approximately 270 amino acid residues. In terms of secondary structure, OspA is made up of 21 anti-parallel single layer beta strands and one alpha helix. 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. 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. | |||
OspA is a unique lipoprotein. It’s elongated fold and protruding ridge gives the surface protein a high degree of mobility and surface exposure, especially Loop 1 in the c-terminus. | |||
== The Elusiveness of OspA == | == The Elusiveness of OspA == | ||
