GTPase KRas

From Proteopedia

Revision as of 18:07, 10 June 2018

spinqualitylabelsall models Structure of human GDP-bound GTPase KRas G12 mutant complex with inhibitor and GDP (PDB entry 4ept) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Disease 3 Relevance 4 Structural highlights Function GTPase KRas (KRas) plays a critical role in the control of cellular growth. Kras stands for Kirsten rat sarcoma virus gene. KRas is a small GTPase that functions as molecular switches by alternating between inactive GDP-bound state and active GTP-bound state[1]. Disease A single mutation of KRas G12C activates KRas and is implicated with various malignancies including lung adenocarcinoma, mutinous adenoma, ductal carcinoma of the pancreas and colorectal carcinoma[2]. KRas mutations are the most common genetic abnormalities in cancer. Relevance KRas inhibition represents an attractive therapeutic strategy for many cancers. Structural highlights The GDP-bound KRas binds a following conformational change of the protein[3]. . . . .

3D Structures of GTPase KRas

Updated on 10-June-2018

References

1. ↑ Milburn MV, Tong L, deVos AM, Brunger A, Yamaizumi Z, Nishimura S, Kim SH. Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins. Science. 1990 Feb 23;247(4945):939-45. PMID:2406906
2. ↑ Shibata H, Ohike N, Norose T, Isobe T, Suzuki R, Imai H, Shiokawa A, Aoki T, Murakami M, Mizukami H, Tanaka JI, Takimoto M. Mucinous Cystic Neoplasms Lined by Abundant Mucinous Epithelium Frequently Involve KRAS Mutations and Malignant Progression. Anticancer Res. 2017 Dec;37(12):7063-7068. doi: 10.21873/anticanres.12178. PMID:29187496 doi:http://dx.doi.org/10.21873/anticanres.12178
3. ↑ Sun Q, Burke JP, Phan J, Burns MC, Olejniczak ET, Waterson AG, Lee T, Rossanese OW, Fesik SW. Discovery of Small Molecules that Bind to K-Ras and Inhibit Sos-Mediated Activation. Angew Chem Int Ed Engl. 2012 May 8. doi: 10.1002/anie.201201358. PMID:22566140 doi:10.1002/anie.201201358