KRAS蛋白包含4個結構域。KRAS蛋白由6條β-折疊鏈和5條-螺旋結構組成，形成兩個主要結構域：G結構域和C端結構域。

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.

KRAS的G結構域由殘基1-166組成，包括GTP結合口袋，該區域對于下游效應物和GTPase激活蛋白之間的相互之間作用至關重要。

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.

G結構域是高度保守的，包括負責GTP-GTP交換的switch Ⅰ和switch Ⅱ區域。

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

C端是一個包含CAAX基序的高變區，引導翻譯后修飾并決定細胞膜錨定，該區域在RAS蛋白的生物活性調控中起著重要作用。/p>

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.

KRAS新藥研發平臺

什么是KRAS?

美迪西助力信諾維抗腫瘤1類新藥XNW14010（小分子KRAS G12C蛋白共價結合抑制劑）獲批臨床