Kentaro Ihara

TL;DR: Structural differences of RhoA contains four insertion or deletion sites with an extra helical subdomain that seems to be characteristic of members of the Rho family, including Rac1, but with several variations in details provide an insight into specific interaction sites with the effectors, as well as with modulators such as guanine nucleotide exchange factor (GEF) and guanines nucleotide dissociation inhibitor (GDI).

TL;DR: A grease-matrix carrier for protein microcrystals is introduced and the structures of lysozyme, glucose isomerase, thaumatin and fatty acid–binding protein type 3 are obtained under ambient conditions at a resolution of or finer than 2 Å.

TL;DR: The crystal structure of a DNA‐binding domain of PHO4 complexed with DNA at 2.8 Å resolution revealed that the domain folds into a basic–helix–loop–helik (bHLH) motif with a long but compact loop that contains a short α‐helical segment.

TL;DR: The structure reveals the antiparallel coiled-coil finger (ACC finger) fold of the effector domain that binds to the Rho specificity-determining regions containing switch I, beta strands B2 and B3, and the C-terminal alpha helix A5, predominantly by specific hydrogen bonds.

TL;DR: It is shown that association of the LCa and LCx ectodomains in vitro depends on monomeric peptidoglycan and that PGRP-LCa recognizes the exposed structural features of a monomersic muropeptide when the latter is bound to and presented by the ectododomain of PGRp-LCx.