9C1A

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

(2024) Acta Crystallogr F Struct Biol Commun 80: 220-227

• PubMed: 39196705 Search on PubMedSearch on PubMed Central
• DOI: https://doi.org/10.1107/S2053230X24007969
• Primary Citation of Related Structures:  
  9C1A, 9C1B


• PubMed 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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Organizational Affiliation: 

Pfizer Boulder Research and Development, 3200 Walnut Street, Boulder, CO 80301, USA.