Catherine Joseph

TL;DR: This work presents the three-dimensional solution structure of the KH module, a sequence motif found in a number of proteins that are known to be in close association with RNA, and suggests a potential surface for RNA binding centered on the loop between the first two helices.

TL;DR: The solution structure of a complex between the calcium-insensitive C-terminal EF-hand domain of α-actinin-2 and the seventh Z-repeat of titin is solved, suggesting that the semi-open conformation is a general structural solution for calcium-independent recognition of EF- hand domains.

TL;DR: The structure of ZASP PDZ is determined by NMR and it is shown that it is a classical class 1 PDZ domain that recognizes the carboxy-terminal sequence of an alpha-actinin-2 calmodulin-like domain with micromolar affinity.

TL;DR: Observations suggest that the mode of binding of Z-repeat 7 to EF34 is similar to that of troponin I to Troponin C and of peptide C20W to calmodulin, which would appear to represent a general alternative binding mode of cal modulin-like domains to target peptides.

TL;DR: In this paper, NMR spectroscopy was used to determine the secondary structure in solution of a KH domain (repeat 5 from vigilin), almost complete assignments were obtained for the ~H and ~SN resonances using uniform ~SN-labeling of the protein combined with homo-nuclear 2D ~HNMR and 3D lSN correlated ~H NMR.