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Characterization of the oligomer structure of recombinant human mannan-binding lectin.
Jensen, Pia H; Weilguny, Dietmar; Matthiesen, Finn; McGuire, Kirsten A; Shi, Lei; Højrup, Peter.
Afiliación
  • Jensen PH; Department of Biochemistry and Molecular Biology, University of Southern Denmark, Odense, Denmark.
J Biol Chem ; 280(12): 11043-51, 2005 Mar 25.
Article en En | MEDLINE | ID: mdl-15653690
ABSTRACT
Mannan-binding lectin (MBL) belongs to a family of proteins called the collectins, which show large differences in their ultrastructures. These differences are believed to be determined by different N-terminal disulfide-bonding patterns. So far only the bonding pattern of two of the simple forms (recombinant rat MBL-C and bovine CL-43) have been determined. Recombinant MBL expressed in human cells was purified, and the structure of the N-terminal region was determined. Preliminary results on human plasma-derived MBL revealed high similarity to the recombinant protein. Here we report the structure of the N-terminal part of recombinant human MBL and present a model to explain the oligomerization pattern. Using a strategy of consecutive enzymatic digestions and matrix-assisted laser desorption ionization mass spectrometry, we succeeded in identifying a number of disulfide-linked peptides from the N-terminal cysteine-rich region. Based on these building blocks, we propose a model that can explain the various oligomeric forms found in purified MBL preparations. Furthermore, the model was challenged by the production of cysteine to serine mutants of the three N-terminally situated cysteines. The oligomerization patterns of these mutants support the proposed model. The model indicates that the polypeptide dimer is the basic unit in the oligomerization.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Lectina de Unión a Manosa Límite: Humans Idioma: En Revista: J Biol Chem Año: 2005 Tipo del documento: Article País de afiliación: Dinamarca
Buscar en Google
Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Lectina de Unión a Manosa Límite: Humans Idioma: En Revista: J Biol Chem Año: 2005 Tipo del documento: Article País de afiliación: Dinamarca
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