9c1b
From Proteopedia
Crystal structure of GDP-bound human M-RAS protein in crystal form II
Structural highlights
DiseaseRASM_HUMAN Noonan syndrome. The disease is caused by variants affecting the gene represented in this entry. FunctionRASM_HUMAN Serves as an important signal transducer for a novel upstream stimuli in controlling cell proliferation. Activates the MAP kinase pathway.[1] [2] Publication Abstract from PubMedM-RAS plays a crucial role in the RAF-MEK signaling pathway. When activated by GTP, M-RAS forms a complex with SHOC2 and PP1C, initiating downstream RAF-MEK signal transduction. In this study, the crystal structure of the GDP-bound human M-RAS protein is presented with two forms of crystal packing. Both the full-length and truncated human M-RAS structures aligned well with the high-confidence section of the AlphaFold2-predicted structure with low r.m.s.d., except for the Switch regions. Despite high sequence similarity to the available mouse M-RAS structure, the full-length human M-RAS structure exhibits unique crystal packing. This inactive human M-RAS structure could offer novel insights for the design of selective compounds targeting M-RAS. Crystal structure of the GDP-bound human M-RAS protein in two crystal forms.,Bester SM, Abrahamsen R, Rodrigues Samora L, Wu WI, Mou TC Acta Crystallogr F Struct Biol Commun. 2024 Sep 1;80(Pt 9):220-227. doi: , 10.1107/S2053230X24007969. Epub 2024 Aug 28. PMID:39196705[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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