Crystal structure of the GDP‐bound human M‐RAS protein in two crystal forms.

M‐RAS plays a crucial role in the RAF–MEK signaling pathway. When activated by GTP, M‐RAS forms a complex with SHOC2 and PP1C, initiating downstream RAF–MEK signal transduction. In this study, the crystal structure of the GDP‐bound human M‐RAS protein is presented with two forms of crystal packing. Both the full‐length and truncated human M‐RAS structures aligned well with the high‐confidence section of the AlphaFold2‐predicted structure with low r.m.s.d., except for the Switch regions. Despite high sequence similarity to the available mouse M‐RAS structure, the full‐length human M‐RAS structure exhibits unique crystal packing. This inactive human M‐RAS structure could offer novel insights for the design of selective compounds targeting M‐RAS. [ABSTRACT FROM AUTHOR]