Multiple sclerosis: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 28: | Line 28: | ||
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/2'>three domains</scene>: an <scene name='Multiple_sclerosis/Ifnr_n_domain_labeled/2'>N-domain</scene>, with two disulfide bonds, a <scene name='Multiple_sclerosis/Ifnr_c_domain_labeled/2'>C-domain</scene>, with one disulfide bond, and a <scene name='Multiple_sclerosis/Ifnr_linker_region_labeled/2'>linker region</scene>. The <scene name='Multiple_sclerosis/Ifnr_termini_labeled/2'>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/2'>eight clashes amongst the domains</scene>, which are all illustrated on the N-terminus region.<ref name="Interferon Receptor Structure">PMID:12842042</ref> | 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/2'>three domains</scene>: an <scene name='Multiple_sclerosis/Ifnr_n_domain_labeled/2'>N-domain</scene>, with two disulfide bonds, a <scene name='Multiple_sclerosis/Ifnr_c_domain_labeled/2'>C-domain</scene>, with one disulfide bond, and a <scene name='Multiple_sclerosis/Ifnr_linker_region_labeled/2'>linker region</scene>. The <scene name='Multiple_sclerosis/Ifnr_termini_labeled/2'>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/2'>eight clashes amongst the domains</scene>, which are all illustrated on the N-terminus region.<ref name="Interferon Receptor Structure">PMID:12842042</ref> | ||
Interferon-α <scene name='Multiple_sclerosis/Ifnawithreceptorcolored/2'>binds</scene> to an interferon receptor mainly with helices C and G. There are many <scene name='Multiple_sclerosis/Ifnawithreceptorintrxns/6'>residues</scene>, shown in ball-and-stick, within 4 angstroms of one another. These residues could form many <scene name='Multiple_sclerosis/ | Interferon-α <scene name='Multiple_sclerosis/Ifnawithreceptorcolored/2'>binds</scene> to an interferon receptor mainly with helices C and G. There are many <scene name='Multiple_sclerosis/Ifnawithreceptorintrxns/6'>residues</scene>, shown in ball-and-stick, within 4 angstroms of one another. These residues could form many <scene name='Multiple_sclerosis/Ifnawithreceptorcolored/3'>different types of bonds</scene>, with hydrogen bonds 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. While interferon-α and -β bind to the same receptors as one another, the affinities with which they bind to IFNAR1 and IFNAR2 differ. While the binding to IFNAR2 is stronger for both in comparison to IFNAR1, interferon-β has a much stronger affinity for IFNAR1 than interferon-α.<ref name="Interferon Receptor Interferon Alpha">PMID:17001036</ref> | ||
===Interferon-β and MS=== | ===Interferon-β and MS=== | ||
