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  • Title: Crystal structure of the GDP-bound human M-RAS protein in two crystal forms.
    Author: Bester SM, Abrahamsen R, Rodrigues Samora L, Wu WI, Mou TC.
    Journal: Acta Crystallogr F Struct Biol Commun; 2024 Sep 01; 80(Pt 9):220-227. PubMed ID: 39196705.
    Abstract:
    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.
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