{"id":33469,"date":"1997-11-12T00:00:00","date_gmt":"1997-11-12T00:00:00","guid":{"rendered":"https:\/\/www.deberes.net\/tesis\/sin-categoria\/modulacion-de-la-union-de-peptidos-por-el-polimorfismo-de-hla-b27\/"},"modified":"1997-11-12T00:00:00","modified_gmt":"1997-11-12T00:00:00","slug":"modulacion-de-la-union-de-peptidos-por-el-polimorfismo-de-hla-b27","status":"publish","type":"post","link":"https:\/\/www.deberes.net\/tesis\/quimica\/modulacion-de-la-union-de-peptidos-por-el-polimorfismo-de-hla-b27\/","title":{"rendered":"Modulacion de la union de peptidos por el polimorfismo de hla-b27."},"content":{"rendered":"<h2>Tesis doctoral de <strong> Fernando Garcia Martinez <\/strong><\/h2>\n<p>Los p\u00e9ptidos presentados por todos los subtipos de hla-b27 estudiados, excepto b*2701, presentan un \u00fanico motivo deanclaje de arg2, aunque no puede descartarse la presentaci\u00f3n minoritaria de p\u00e9ptidos con motivos de anclaje diferentes.  la estructura de la subcavidad b de hla-b27 estudiados, excepto b*2701, presentan un \u00fanico motivo de anclaje de arg2, aunque no puede descartarse la presentaci\u00f3n minoritaria de p\u00e9ptidos con motivos de anclaje diferentes.  la estructura de la subcavidad b de hla-b27 determina la capacidad de unir \u00f3ptimamente p\u00e9ptidos con arg2. La modificaci\u00f3n de la estructura de esta subcavidad disminuye la selectividad por este residuo y favorece la entrada de otros, en particular gln. Los motivos pept\u00eddicos del subtipo b*2703 son similares a los de b*2705. En b*2703 la interacci\u00f3n de arg2 con la subcavidad b es mas n-terminal con la subcavidad a es m\u00e1s d\u00e9bil que en b*2705. Estos datos son la asociaci\u00f3n de b*2703 a la espondilitis anqulipoy\u00e9tica. El polimorfismo de b*2701, influye de forma directa en el motivo pept\u00eddico de anclaje en posici\u00f3n 2, permitiendo la uni\u00f3n in vivo de p\u00e9ptidos con arg2 y gln2. Este efecto es debido al residuo y74. Existe una correlaci\u00f3n entre la incapacidad del subtipo b*2706 de presentar p\u00e9ptidos con tyr c-terminal y su no asociaci\u00f3n con la ea. B*2701, 04, y 06 pero no b*2703, son capaces de unir in vivo un p\u00e9ptido de la propia mol\u00e9cula de hla-b27 que comprende las posiciones 169-179, homologo a p\u00e9ptidos de enterobacterias. La presentaci\u00f3n de este p\u00e9ptido no se correlaciona con la asociaci\u00f3n de los subtipos a la ea.  la disparidad antig\u00e9nica del subtipo b*2710 con respecto a b*2705 no es debida a la presentaci\u00f3n de p\u00e9ptidos muy diferentes ni a diferencias conformacionales de los p\u00e9ptidos unidos, sino a un efecto directo del cambio v152e sobre la interacci\u00f3n con el tcr.<\/p>\n<p>&nbsp;<\/p>\n<h3>Datos acad\u00e9micos de la tesis doctoral \u00ab<strong>Modulacion de la union de peptidos por el polimorfismo de hla-b27.<\/strong>\u00ab<\/h3>\n<ul>\n<li><strong>T\u00edtulo de la tesis:<\/strong>\u00a0 Modulacion de la union de peptidos por el polimorfismo de hla-b27. <\/li>\n<li><strong>Autor:<\/strong>\u00a0 Fernando Garcia Martinez <\/li>\n<li><strong>Universidad:<\/strong>\u00a0 Aut\u00f3noma de Madrid<\/li>\n<li><strong>Fecha de lectura de la tesis:<\/strong>\u00a0 11\/12\/1997<\/li>\n<\/ul>\n<p>&nbsp;<\/p>\n<h3>Direcci\u00f3n y tribunal<\/h3>\n<ul>\n<li><strong>Director de la tesis<\/strong>\n<ul>\n<li>Jos\u00e9 Antonio L\u00f3pez De Castro<\/li>\n<\/ul>\n<\/li>\n<li><strong>Tribunal<\/strong>\n<ul>\n<li>Presidente del tribunal: manuel Ortiz de landazuri <\/li>\n<li>Carlos Lopez larrea (vocal)<\/li>\n<li>Antonio Ortiz alonso (vocal)<\/li>\n<li>dolores Jaraquemada p\u00e9rez de guzm\u00e1n (vocal)<\/li>\n<\/ul>\n<\/li>\n<\/ul>\n<p>&nbsp;<\/p>\n","protected":false},"excerpt":{"rendered":"<p>Tesis doctoral de Fernando Garcia Martinez Los p\u00e9ptidos presentados por todos los subtipos de hla-b27 estudiados, excepto b*2701, presentan un [&hellip;]<\/p>\n","protected":false},"author":1,"featured_media":0,"comment_status":"open","ping_status":"open","sticky":false,"template":"","format":"standard","meta":{"site-sidebar-layout":"default","site-content-layout":"","ast-site-content-layout":"","site-content-style":"default","site-sidebar-style":"default","ast-global-header-display":"","ast-banner-title-visibility":"","ast-main-header-display":"","ast-hfb-above-header-display":"","ast-hfb-below-header-display":"","ast-hfb-mobile-header-display":"","site-post-title":"","ast-breadcrumbs-content":"","ast-featured-img":"","footer-sml-layout":"","theme-transparent-header-meta":"","adv-header-id-meta":"","stick-header-meta":"","header-above-stick-meta":"","header-main-stick-meta":"","header-below-stick-meta":"","astra-migrate-meta-layouts":"default","ast-page-background-enabled":"default","ast-page-background-meta":{"desktop":{"background-color":"var(--ast-global-color-4)","background-image":"","background-repeat":"repeat","background-position":"center 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