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Theoretical representation explaining protein aggregation in stromal “spaces”.

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posted on 01.02.2016, 20:57 by Christina S. Kamma-Lorger, Christian Pinali, Juan Carlos Martínez, Jon Harris, Robert D. Young, Cecilie Bredrup, Eva Crosas, Marc Malfois, Eyvind Rødahl, Keith M. Meek, Carlo Knupp

The mutation in Decorin in the case of CSCD did not affect the protein’s ability to form dimers, but prevented it from interacting with collagen and caused it to subsequently aggregate in lamellar gaps in the diseased stroma. The aggregated molecules formed anti-parallel associations. The regions with the protein cores are unstained and invisible, whereas the two fold axes are where the red diamonds are.

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