Structure of a truncated form of leucine zipper II of JIP3 reveals an unexpected antiparallel coiled-coil arrangement

This study highlights that N-terminal truncation of LZII can change its coiled-coil orientation without affecting its overall stability. Further, a conserved buried asparagine residue was pinpointed as a possible structural determinant for this dramatic structural rearrangement. Thus, LZII of JIP3/4 is a versatile structural motif, modifications of which can impact partner recognition and thus biological function.

Source: Acta Crystallographica Section F - February 16, 2016 Category: Biochemistry Authors: Llinas, P.Chenon, M.Nguyen, T.Q.Moreira, C.de Régibus, A.Coquard, A.Ramos, M.J.Guérois, R.Fernandes, P.A.Ménétrey, J. Tags: JIP3 JIP4 leucine zipper II crystal structure molecular dynamics antiparallel coiled coil buried asparagine research communications Source Type: research