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KRAS protein contains 4 domains.KRAS protein is made up of 6 beta-strands and 5 alpha-helicies, which form two major domains: G-domain and C-terminal.
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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.
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The G domain is highly conserved and contains switch ¢ñ and switch ¢ò loops, which are responsible for GDP-GTP exchange.
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The C-terminal, a hypervariable region including the CAAX 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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