Lactoferrin and transferrin: functional variations on a common structural framework.

Baker, Edward N; Baker, Heather M; Kidd, Richard D

Baker, Edward N; Baker, Heather M; Kidd, Richard D.

Afiliación

Baker EN; School of Biological Sciences, University of Auckland, New Zealand. ted.baker@auckland.ac.nz

Biochem Cell Biol ; 80(1): 27-34, 2002.

Article en En | MEDLINE | ID: mdl-11908640

RESUMEN

Lactoferrin shares many structural and functional features with serum transferrin, including an ability to bind iron very tightly, but reversibly, a highly-conserved three-dimensional structure, and essentially identical iron-binding sites. Nevertheless, lactoferrin has some unique properties that differentiate it: an ability to retain iron to much lower pH, a positively charged surface, and other surface features that give it additional functions. Here, we review the structural basis for these similarities and differences, including the importance of dynamics and conformational change, and specific interactions that regulate iron binding and release.

Asunto(s)

Lactoferrina/química; Lactoferrina/metabolismo; Transferrina/química; Transferrina/metabolismo; Animales; Sitios de Unión; Humanos; Hierro/metabolismo; Modelos Moleculares; Unión Proteica; Conformación Proteica; Electricidad Estática; Relación Estructura-Actividad

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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Transferrina / Lactoferrina Límite: Animals / Humans Idioma: En Revista: Biochem Cell Biol Asunto de la revista: BIOQUIMICA Año: 2002 Tipo del documento: Article País de afiliación: Nueva Zelanda Pais de publicación: Canadá

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