Multiple sclerosis: Difference between revisions
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<scene name='Multiple_sclerosis/Ifnr_n_domain_labeled/1'>N-domain, with two disulfide bonds</scene>, a <scene name='Multiple_sclerosis/Ifnr_c_domain_labeled/1'>C-domain, with one disulfide bond</scene>, 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>.<ref name="Interferon Receptor Structure">PMID:12842042</ref> | <scene name='Multiple_sclerosis/Ifnr_n_domain_labeled/1'>N-domain, with two disulfide bonds</scene>, a <scene name='Multiple_sclerosis/Ifnr_c_domain_labeled/1'>C-domain, with one disulfide bond</scene>, 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>.<ref name="Interferon Receptor Structure">PMID:12842042</ref> | ||
Interferon-α <scene name='Multiple_sclerosis/Ifnawithreceptorcolored/1'>binds</scene> to an interferon receptor mainly with helices C and G. There are many <scene name='Multiple_sclerosis/Ifnawithreceptorintrxns/2'>residues</scene> within 4 angstroms of one another. These residues could form many <scene name='Multiple_sclerosis/Ifnawithreceptorintrxns/5'>different types of bonds</scene>, illustrated in white dotted lines. Given that interferon-α does not undergo many structural changes upon binding to interferon receptor II, Quadt-Akabayov et al. have concluded that the binding mechanism is similar to that of a lock and key. | Interferon-α <scene name='Multiple_sclerosis/Ifnawithreceptorcolored/1'>binds</scene> to an interferon receptor mainly with helices C and G. There are many <scene name='Multiple_sclerosis/Ifnawithreceptorintrxns/2'>residues</scene> within 4 angstroms of one another. These residues could form many <scene name='Multiple_sclerosis/Ifnawithreceptorintrxns/5'>different types of bonds</scene>, illustrated in white dotted lines. Given that interferon-α does not undergo many structural changes upon binding to interferon receptor II, Quadt-Akabayov et al. have concluded that the binding mechanism is similar to that of a lock and key.<ref name="Interferon Receptor Interferon Alpha">PMID:17001036</ref> | ||
===Interferon Beta and MS=== | ===Interferon Beta and MS=== | ||