G09SecL04Tpc2: Difference between revisions

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== 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.

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. 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.

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 definitely 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.

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 ==

G09SecL04Tpc2: Difference between revisions

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@@ Line 14: / Line 14: @@
 == 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.
+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. 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.
+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 definitely 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.
-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 ==