| Autor: |
Vanderhaegen, Saskia, Fislage, Marcus, Domanska, Katarzyna, Versées, Wim, Pardon, Els, Bellotti, Vittorio, Steyaert, Jan |
| Zdroj: |
Protein Science: A Publication of the Protein Society; Oct2013, Vol. 22 Issue 10, p1349-1357, 9p |
| Abstrakt: |
To investigate early intermediates of β2-microglobulin (β2m) amyloidogenesis, we solved the structure of β2m containing the amyloidogenic Pro32Gly mutation by X-ray crystallography. One nanobody (Nb24) that efficiently blocks fibril elongation was used as a chaperone to co-crystallize the Pro32Gly β2m monomer under physiological conditions. The complex of P32G β2m with Nb24 reveals a trans peptide bond at position 32 of this amyloidogenic variant, whereas Pro32 adopts the cis conformation in the wild-type monomer, indicating that the cis to trans isomerization at Pro32 plays a critical role in the early onset of β2m amyloid formation. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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