G09SecL04Tpc2: Difference between revisions

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<scene name='G09SecL04Tpc2/Newfirst/1'>Reset Model</scene>

Outer Surface Protein A has approximately 270 amino acid residues.<ref name=art3>PMID:11183781</ref> In terms of <scene name='G09SecL04Tpc2/Startospa/3'>secondary structure</scene>, OspA is made up of 21 [http://en.wikipedia.org/wiki/Antiparallel_(biochemistry) 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/Newfirst/2'>n-terminal sandwich</scene>, ~~<scene name='G09SecL04Tpc2/Newfirst/3'>a~~ central sheet~~</scene>~~, and a ~~<scene name='G09SecL04Tpc2/Newfirst/4'>~~c-terminal barrel domain~~</scene>~~. 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 <scene name='G09SecL04Tpc2/Startospa/3'>secondary structure</scene>, OspA is made up of 21 [http://en.wikipedia.org/wiki/Antiparallel_(biochemistry) anti-parallel] single layer beta strands (gold) and one alpha helix (magenta). <ref name=art3>PMID:11183781</ref>OspA has three major components to its structure: an <scene name='G09SecL04Tpc2/Newfirst/2'>n-terminal sandwich</scene>, central sheet, and a c-terminal barrel domain. 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 <scene name='G09SecL04Tpc2/Newfirst/3'>a central sheet</scene>. Lastly, the <scene name='G09SecL04Tpc2/Newfirst/4'>c-terminal </scene> is nicknamed 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: <scene name='G09SecL04Tpc2/3loops/1'>loop 1</scene> contains residues 203-220; <scene name='G09SecL04Tpc2/3loops/2'>loop 2</scene> contains residues 224-233; <scene name='G09SecL04Tpc2/3loops/3'>loop 3</scene> contains residues 246-257. These <scene name='G09SecL04Tpc2/3loops/4'>3 loops</scene> define the LA-2 (antibody) [http://en.wikipedia.org/wiki/Epitope epitope] discussed below. 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 surface exposure. Loops 2 and 3 tend to be more conserved.

G09SecL04Tpc2: Difference between revisions

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@@ Line 12: / Line 12: @@
 <scene name='G09SecL04Tpc2/Newfirst/1'>Reset Model</scene>
-Outer Surface Protein A has approximately 270 amino acid residues.<ref name=art3>PMID:11183781</ref> In terms of <scene name='G09SecL04Tpc2/Startospa/3'>secondary structure</scene>, OspA is made up of 21 [http://en.wikipedia.org/wiki/Antiparallel_(biochemistry) 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/Newfirst/2'>n-terminal sandwich</scene>, <scene name='G09SecL04Tpc2/Newfirst/3'>a central sheet</scene>, and a <scene name='G09SecL04Tpc2/Newfirst/4'>c-terminal barrel domain</scene>. 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 <scene name='G09SecL04Tpc2/Startospa/3'>secondary structure</scene>, OspA is made up of 21 [http://en.wikipedia.org/wiki/Antiparallel_(biochemistry) anti-parallel] single layer beta strands (gold) and one alpha helix (magenta). <ref name=art3>PMID:11183781</ref>OspA has three major components to its structure: an <scene name='G09SecL04Tpc2/Newfirst/2'>n-terminal sandwich</scene>, central sheet, and a c-terminal barrel domain. 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 <scene name='G09SecL04Tpc2/Newfirst/3'>a central sheet</scene>. Lastly, the <scene name='G09SecL04Tpc2/Newfirst/4'>c-terminal </scene> is nicknamed 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: <scene name='G09SecL04Tpc2/3loops/1'>loop 1</scene> contains residues 203-220; <scene name='G09SecL04Tpc2/3loops/2'>loop 2</scene> contains residues 224-233; <scene name='G09SecL04Tpc2/3loops/3'>loop 3</scene> contains residues 246-257. These <scene name='G09SecL04Tpc2/3loops/4'>3 loops</scene> define the LA-2 (antibody) [http://en.wikipedia.org/wiki/Epitope epitope] discussed below. 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 surface exposure. Loops 2 and 3 tend to be more conserved.