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Estructura de la Proteína de la Insulina

Por el Dr. Ananya Mandal, DOCTOR EN MEDICINA

La estructura de la insulina es diferente entre diversa especie de animales. Sin

Embargo, esencialmente es un encadenamiento de la proteína que es similar en granmedida entre animales.

La insulina Humana está la más cercana de estructura y de la función con la insulina(porcina) de la vaca (bovina) o del lingote. La insulina Bovina difiere de ser humano ensolamente tres residuos del aminoácido, y de la insulina porcina en uno.

La Insulina de algunos invertebrados e incluso pescados puede ser clínico útil en sereshumanos mientras que poseen varias semejanzas.

Estructura de la Insulina

La insulina Normal que es biológicamente activa es monomérica o existe como únicamolécula. Tiene dos encadenamientos largos del aminoácido o encadenamientos delpolipéptido. Los encadenamientos son A de cadena con 21 aminoácidos y elencadenamiento B con 30 aminoácidos.

Dos puentes de disulfuro (residuos A7 a B7, y A20 a B19) covalente conectan losencadenamientos, y encadenan A contienen un puente de disulfuro interno (residuos A6a A11). Estas juntas son similares en todos los formularios mamíferos de la insulina.

Cuando está secretada la insulina ensambla en dos a los reductores de luz delformulario y entonces en seis a los hexamers del formulario. Esta combinación ocurreen presencia del cinc.

El péptido encadena entonces el formulario los formularios dimensionales ytridimensionales de 2. Cada Uno de estas estructuras de 3 dimensiones tiene treshélices y tres puentes de disulfuro conservados. Esto es un doblez básico. Este doblezbásico está presente en todas las piezas de la familia del péptido de la insulina.

En la base o el centro de las moléculas es un hidrofóbico o un “agua-odio” o un áreadel hidrófugo. Éstos atado de residuos hidrofóbicos en el centro contribuyen a laestabilidad de la proteína. La Estabilidad también es prestada por los puentes dedisulfuro.

Rodeando su base, el monómero tiene dos superficies no polares extensas. Una deellas es plano que es aromático y consigue soterrado cuando hay una formación dedimero. La otra superficie es más extensa y desaparece cuando se forma un hexamer.Esto se llama la estructura de cuaternario de la insulina.

Estructura en la síntesis

En las células beta del páncreas, la molécula de la insulina se produce originalmentecomo única molécula (preproinsulin) integrada por 110 aminoácidos. Pasa a través delretículo endoplásmico y 24 aminoácidos (“el péptido de señal”) son quitados por laacción enzimática a partir de un extremo del encadenamiento, saliendo de otroformulario (favorable-insulina) detrás.

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El proinsulin plegable y ata para dar a la molécula su estructura final. Entonces elproinsulin pasa en las vesículas florecidas lejos del cuerpo de Golgi.

La sección central (“el encadenamiento de C”) de 33 aminoácidos es quitada DespuésDe Eso por la acción del convertase 1 y 2 del prohormone de las enzimas,convirtiéndolo en la estructura final con 2 encadenamientos, A y B. 2 aminoácidos sonquitados Más Lejos por otra carboxipeptidasa E. de la enzima.

En abril Cashin-Garbutt Revisado, VAGOS Hons (Cantab)

Fuentes

1. http://www.japi.org/july2007/suppliment/19.pdf 2. http://www.uta.edu/biology/wilk/classnotes/endocrinology/Insulin.pdf

3. http://www.biotopics.co.uk/as/insulinproteinstructure.html4. http://www.betacell.org/content/articleview/article_id/8/

Lectura Adicional

¿Cuál es Insulina?Gen de la InsulinaSíntesis de la InsulinaHipoglucemia de la InsulinaEnfermedades de la InsulinaMedicación de la InsulinaDescubrimiento de la Insulina

Last Updated: Mar 30, 2013

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