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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.
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.