作者: Jae-Hee Jeong , Kwang-Hoon Lee , Young-Mi Kim , Do-Hyung Kim , Byung-Ha Oh
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摘要: The heterodimeric Rag GTPases consisting of RagA (or RagB) and RagC RagD) are the key regulator activating target rapamycin complex 1 (TORC1) in response to level amino acids. heterodimer between GTP-loaded RagA/B GDP-loaded RagC/D is most active form that binds Raptor leads activation TORC1. Here, we present crystal structure Gtr1pGTP-Gtr2pGDP, yeast GTPase heterodimer. reveals GTP-to-GDP conversion on Gtr2p results a large conformational transition this subunit, including scale rearrangement long segment whose corresponding region involved binding Raptor. In addition, two domains brought contact with each other, but without causing any change Gtr1p subunit. These features explain how nucleotide-bound statuses subunits switch affinity off.