Multiple sclerosis: Difference between revisions

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===Interferon-α, Interferon-β, and Interferon Receptors 1 & 2 ===

Since a PDB reference does not exist for interferon-β interacting with interferon receptors 1 or 2, and a multitude of files exist on <scene name='Multiple_sclerosis/Ifna/1'>interferon-α</scene> interacting with the receptor, a comparison to interferon-α will be made prior to demonstrating the types of bonding that occur between the interferon and its receptor. To see more information regarding interferons, please visit the [[Interferons]] site.

Since a PDB reference does not exist for interferon-β interacting with interferon receptors 1 or 2, and a multitude of files exist on <scene name='Multiple_sclerosis/Ifna/5'>interferon-α</scene> interacting with the receptor, a comparison to interferon-α will be made prior to demonstrating the types of bonding that occur between the interferon and its receptor. To see more information regarding interferons, please visit the [[Interferons]] site.

Interferon-α has a 31% sequence homology to interferon-β. It, too, has many <scene name='Multiple_sclerosis/Ifna_labeled/1'>identifiable regions</scene> with two <scene name='Multiple_sclerosis/Ifna_disulfide_bonds/1'>disulfide bonds</scene>: one between the <scene name='Multiple_sclerosis/Ifna_disulfide_bondsn-e/1'>N-terminus and Helix E</scene>, and the other between <scene name='Multiple_sclerosis/Ifna_disulfide_bonds_ab-g/1'>Loop AB and Helix G</scene>. It has seven <scene name='Multiple_sclerosis/Ifna_alphahelices/1'>alpha helices</scene>, as compared to the five of interferon-β, and therefore has ~~several~~ more <scene name='Multiple_sclerosis/Ifna_loops_regions/1'>loop regions.</scene> The helices A, C, and F run <scene name='Multiple_sclerosis/Ifna_parallelacf/2'>parallel</scene> to one another, and <scene name='Multiple_sclerosis/Ifna_antiparallel/1'>anti-parallel</scene> to B, E, and G which run <scene name='Multiple_sclerosis/Ifna_parallel_beg/2'>parallel</scene> to each other.<scene name='Multiple_sclerosis/Ifna_notparalleltoanyoned/1'>Helix D</scene> does not run parallel or anti-parallel to either set, but rather runs at a 45-90 degree angle to them. Helix A consists of residues 10-12; Helix B of 40-43; Helix C of 53-68; Helix D of 70-75; Helix E of 78-100; Helix F of 109-132; and Helix G of 137-158.

Interferon-α has a 31% sequence homology to interferon-β. It too has many <scene name='Multiple_sclerosis/Ifna_labeled/2'>identifiable regions</scene> with two <scene name='Multiple_sclerosis/Ifna_disulfide_bonds/2'>disulfide bonds</scene>: one between the <scene name='Multiple_sclerosis/Ifna_disulfide_bondsn-e/2'>N-terminus and Helix E</scene>, and the other between <scene name='Multiple_sclerosis/Ifna_disulfide_bonds_ab-g/2'>Loop AB and Helix G</scene>. It has seven <scene name='Multiple_sclerosis/Ifna_alphahelices/2'>alpha helices</scene>, as compared to the five of interferon-β, and therefore has more <scene name='Multiple_sclerosis/Ifna_loops_regions/2'>loop regions.</scene> The helices A, C, and F run <scene name='Multiple_sclerosis/Ifna_parallelacf/3'>parallel</scene> to one another, and <scene name='Multiple_sclerosis/Ifna_antiparallel/2'>anti-parallel</scene> to B, E, and G which run <scene name='Multiple_sclerosis/Ifna_parallel_beg/3'>parallel</scene> to each other.<scene name='Multiple_sclerosis/Ifna_notparalleltoanyoned/2'>Helix D</scene> does not run parallel or anti-parallel to either set, but rather runs at a 45-90 degree angle to them. Helix A consists of residues 10-12; Helix B of 40-43; Helix C of 53-68; Helix D of 70-75; Helix E of 78-100; Helix F of 109-132; and Helix G of 137-158.

Interferons-α and -β interact with a receptor at the cell surface.<ref>[http://www.jbc.org/content/282/28/20045.full?sid=cbf08059-44d4-4957-8ea7-0351cab9c2ac] Samuel, C.E. "Interferons, Interferon Receptors, Signal Transducer and Transcriptional Activators, and Inteferon Regulatory Factors." ''J Biol Chem'' 2007 282: 20045-20046. First Published on May 14, 2007, doi:10.1074/jbc.R700025200</ref> This receptor has <scene name='Multiple_sclerosis/Ifnr_domains_labeled/1'>three domains</scene>: an <scene name='Multiple_sclerosis/Ifnr_n_domain_labeled/1'>N-domain</scene>, with two disulfide bonds, a <scene name='Multiple_sclerosis/Ifnr_c_domain_labeled/1'>C-domain</scene>, with one disulfide bond, and a <scene name='Multiple_sclerosis/Ifnr_linker_region_labeled/1'>linker region</scene>. The <scene name='Multiple_sclerosis/Ifnr_termini_labeled/1'>termini regions</scene> of the receptor have no secondary structure, allowing for some serious flexibility, leading to <scene name='Multiple_sclerosis/Ifnr_clash_n-c/1'>eight clashes amongst the domains</scene>, which are all illustrated on the N-terminus region.<ref name="Interferon Receptor Structure">PMID:12842042</ref>

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@@ Line 22: / Line 22: @@
 ===Interferon-α, Interferon-β, and Interferon Receptors 1 & 2 ===
-Since a PDB reference does not exist for interferon-β interacting with interferon receptors 1 or 2, and a multitude of files exist on <scene name='Multiple_sclerosis/Ifna/1'>interferon-α</scene> interacting with the receptor, a comparison to interferon-α will be made prior to demonstrating the types of bonding that occur between the interferon and its receptor. To see more information regarding interferons, please visit the [[Interferons]] site.
+Since a PDB reference does not exist for interferon-β interacting with interferon receptors 1 or 2, and a multitude of files exist on <scene name='Multiple_sclerosis/Ifna/5'>interferon-α</scene> interacting with the receptor, a comparison to interferon-α will be made prior to demonstrating the types of bonding that occur between the interferon and its receptor. To see more information regarding interferons, please visit the [[Interferons]] site.
-Interferon-α has a 31% sequence homology to interferon-β. It, too, has many <scene name='Multiple_sclerosis/Ifna_labeled/1'>identifiable regions</scene> with two <scene name='Multiple_sclerosis/Ifna_disulfide_bonds/1'>disulfide bonds</scene>: one between the <scene name='Multiple_sclerosis/Ifna_disulfide_bondsn-e/1'>N-terminus and Helix E</scene>, and the other between <scene name='Multiple_sclerosis/Ifna_disulfide_bonds_ab-g/1'>Loop AB and Helix G</scene>. It has seven <scene name='Multiple_sclerosis/Ifna_alphahelices/1'>alpha helices</scene>, as compared to the five of interferon-β, and therefore has several more <scene name='Multiple_sclerosis/Ifna_loops_regions/1'>loop regions.</scene> The helices A, C, and F run <scene name='Multiple_sclerosis/Ifna_parallelacf/2'>parallel</scene> to one another, and <scene name='Multiple_sclerosis/Ifna_antiparallel/1'>anti-parallel</scene> to B, E, and G which run <scene name='Multiple_sclerosis/Ifna_parallel_beg/2'>parallel</scene> to each other.<scene name='Multiple_sclerosis/Ifna_notparalleltoanyoned/1'>Helix D</scene> does not run parallel or anti-parallel to either set, but rather runs at a 45-90 degree angle to them. Helix A consists of residues 10-12; Helix B of 40-43; Helix C of 53-68; Helix D of 70-75; Helix E of 78-100; Helix F of 109-132; and Helix G of 137-158.
+Interferon-α has a 31% sequence homology to interferon-β. It too has many <scene name='Multiple_sclerosis/Ifna_labeled/2'>identifiable regions</scene> with two <scene name='Multiple_sclerosis/Ifna_disulfide_bonds/2'>disulfide bonds</scene>: one between the <scene name='Multiple_sclerosis/Ifna_disulfide_bondsn-e/2'>N-terminus and Helix E</scene>, and the other between <scene name='Multiple_sclerosis/Ifna_disulfide_bonds_ab-g/2'>Loop AB and Helix G</scene>. It has seven <scene name='Multiple_sclerosis/Ifna_alphahelices/2'>alpha helices</scene>, as compared to the five of interferon-β, and therefore has more <scene name='Multiple_sclerosis/Ifna_loops_regions/2'>loop regions.</scene> The helices A, C, and F run <scene name='Multiple_sclerosis/Ifna_parallelacf/3'>parallel</scene> to one another, and <scene name='Multiple_sclerosis/Ifna_antiparallel/2'>anti-parallel</scene> to B, E, and G which run <scene name='Multiple_sclerosis/Ifna_parallel_beg/3'>parallel</scene> to each other.<scene name='Multiple_sclerosis/Ifna_notparalleltoanyoned/2'>Helix D</scene> does not run parallel or anti-parallel to either set, but rather runs at a 45-90 degree angle to them. Helix A consists of residues 10-12; Helix B of 40-43; Helix C of 53-68; Helix D of 70-75; Helix E of 78-100; Helix F of 109-132; and Helix G of 137-158.
 Interferons-α and -β interact with a receptor at the cell surface.<ref>[http://www.jbc.org/content/282/28/20045.full?sid=cbf08059-44d4-4957-8ea7-0351cab9c2ac] Samuel, C.E. "Interferons, Interferon Receptors, Signal Transducer and Transcriptional Activators, and Inteferon Regulatory Factors." ''J Biol Chem'' 2007 282: 20045-20046. First Published on May 14, 2007, doi:10.1074/jbc.R700025200</ref> This receptor has <scene name='Multiple_sclerosis/Ifnr_domains_labeled/1'>three domains</scene>: an <scene name='Multiple_sclerosis/Ifnr_n_domain_labeled/1'>N-domain</scene>, with two disulfide bonds, a <scene name='Multiple_sclerosis/Ifnr_c_domain_labeled/1'>C-domain</scene>, with one disulfide bond, and a <scene name='Multiple_sclerosis/Ifnr_linker_region_labeled/1'>linker region</scene>. The <scene name='Multiple_sclerosis/Ifnr_termini_labeled/1'>termini regions</scene> of the receptor have no secondary structure, allowing for some serious flexibility, leading to <scene name='Multiple_sclerosis/Ifnr_clash_n-c/1'>eight clashes amongst the domains</scene>, which are all illustrated on the N-terminus region.<ref name="Interferon Receptor Structure">PMID:12842042</ref>