Understanding the role of the Radish protein

  • Radish sequence analysis: large chunks of disorder, with the last 100AA of possibly tight/defined structure (suggested by compositional bias – this region might be responsible for precise binding/recognition to nucleic acid); there’s a lot of short sequence motifs in Radish protein, but given
    compositional bias of the whole protein, it’s impossible to distinguish true from false ones.
  • structure prediction isn’t feasible (intrinsic disorder), however as soon we have cluster in place (around end of June), together with a friend we plan to do some serious studies on dynamics of disordered proteins – Radish, one human and one cattle proteins are chosen for test cases; the aim of these studies in case of Radish is to see if we can distinguish between linear motifs binding to proteins and motifs binding to nucleic acids (it’s not clear from the sequence).
  • network analysis does not confirm sequence similarity (or rather compositional similarity) to human Serine/arginine repetitive matrix protein 2 – both proteins, according to biological databases, have completely different functional network around; however, given how little is known about functional partners of Radish (hard data available only for connections with sPLA2 and Rac1), it’s possible analogy to human subsystem will reappear – especially, that there’s little hard data for SRRM2 too modeling of the subsystem didn’t work yet because there’s not enough data or I didn’t read enough papers – I don’t have enough connections and enough players to guess what Radish can do at a molecular level.

News concerning this project

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