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TitleStability improvement of the fatty acid binding protein Sm14 from S. mansoni by Cys replacement: Structural and functional characterization of a vaccine candidate.
Journal, issue, pagesBiochim. Biophys. Acta, Vol. 1794, Page 655-662, Year 2009
Publish dateApr 26, 2007 (structure data deposition date)
AuthorsRamos, C.R. / Spisni, A. / Oyama, S. / Sforca, M.L. / Ramos, H.R. / Vilar, M.M. / Alves, A.C. / Figueredo, R.C. / Tendler, M. / Zanchin, N.I. ...Ramos, C.R. / Spisni, A. / Oyama, S. / Sforca, M.L. / Ramos, H.R. / Vilar, M.M. / Alves, A.C. / Figueredo, R.C. / Tendler, M. / Zanchin, N.I. / Pertinhez, T.A. / Ho, P.L.
External linksBiochim. Biophys. Acta / PubMed:19150418
MethodsNMR (solution)
Structure data

PDB-2poa:
Schistosoma mansoni Sm14 Fatty Acid-Binding Protein: improvement of protein stability by substitution of the single Cys62 residue
Method: SOLUTION NMR

Source
  • schistosoma mansoni (invertebrata)
KeywordsLIPID BINDING PROTEIN / Schistosoma mansoni / fatty acid binding protein / site directed mutagenesis / protein stability / molecular dynamics / vaccine antigen

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