Structure of KRAS

KRAS protein contains four domains.

KRAS protein is made up of six beta-strands (forming the protein core) and five alpha-helices, which form two major domains: G-domain and C-terminal.

The G domain of KRAS, comprised of residues 1-166, includes the GTP-binding pocket, a region within which is essential for the interactions between the putative downstream effectors and GTPase-activating proteins.

The G domain is highly conserved and contains switch I and switch II loops, which are responsible for GDP-GTP exchange.

The C-terminal, a hypervariable region including the CAAX (C=cysteine, A=any aliphatic amino acid, X=any amino acid) motif, guides posttranslational modifications and determines plasma membrane anchoring.

This region plays an important role in the regulation of the biological activity of RAS protein.

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  KRAS-targeted Drugs R&D Service
  KRAS-targeted Drugs R&D Service

  In the formulation of KRAS integrated research plan, Medicilon has in-depth communication with customers. The backbone of scientific research has combined the characteristics of each case with years of practical experience and technical accumulation, and carefully submitted high-quality experimental plans and results to customers. Medicilon provides KRAS-targeted drug discovery, CMC research (API + formulation), pharmacodynamics research, PK study, safety evaluation and other services.