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Functional characterization of Val60, a key residue involved in the membrane‐oligomerization of fragaceatoxin C, an actinoporin from Actinia fragacea
Author(s) -
Morante Koldo,
Caaveiro Jose M.M.,
Viguera Ana Rosa,
Tsumoto Kouhei,
González-Mañas Juan Manuel
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.06.012
Subject(s) - membrane , residue (chemistry) , biophysics , chemistry , toxin , biochemistry , biology
To gain insight into the mechanism of toxin oligomerization, different point mutations have been introduced at this position. Functional characterization of the muteins suggests that Val60 represents a hot‐spot where the introduction of mutations hinders protein assembly and reduces the overall affinity for membranes.