Effects of pathological mutations on the stability of a conserved amino acid triad in retinoschisin

Franca Fraternali, Luigi Cavallo, Giovanna Musco*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

29 Scopus citations


A three-dimensional model has been calculated for the discoidin domain of retinoschisin (RS1), the protein involved in the X-linked juvenile retinoschisis. The model allows for a mapping of the pathological retinoschisis missense mutations and a rationale for the structural effects of an evolutionary conserved surface exposed triad (W122-R200-W163). Molecular dynamics simulations of the triad mutants models, together with ab initio energy calculations of the complexes corresponding to the triad show that the observed pathological mutations sensibly destabilize local interactions and the entire fold. Moreover the presented model reveals evidence of a putative site for membrane association.

Original languageEnglish (US)
Pages (from-to)21-26
Number of pages6
JournalFEBS Letters
Issue number1-3
StatePublished - Jun 5 2003
Externally publishedYes


  • Ab initio energy calculation
  • Discoidin domain
  • Membrane binding site
  • Molecular dynamics
  • Pathological mutation
  • Retinoschisis

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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