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• W2076012105 abstract "The tumor suppressor DLC2 (Deleted in Liver Cancer -2) participates in cell signaling at the mitochondrial membrane. DLC2 is characterized by a SAM (sterile alpha motif) domain, a Rho GTPase activating protein (GAP) domain, and a START lipid transfer domain.Towards understanding the function of DLC2, we have solved the NMR solution structure of the SAM domain. The DLC2-SAM domain structure reveals an atypical four-helix composition that is distinct from the five-helix SAM domain structures that have been determined to date. From structural alignments, helix 3 of the canonical SAM domain appears to be replaced by shorter, extended secondary structure that follows a similar path. Another difference is demonstrated by helices 1 and 2 that form a helical hairpin that is situated approximately parallel to the canonical helix 5.The DLC2-SAM domain adopts a structure that is topologically more similar to an anti-parallel four-helix bundle than a canonical SAM domain. This alternate topology may allow the DLC2-SAM domain to interact with a novel set of ligands." @default.
• W2076012105 created "2016-06-24" @default.
• W2076012105 creator A5028734818 @default.
• W2076012105 creator A5074685484 @default.
• W2076012105 date "2007-01-01" @default.
• W2076012105 modified "2023-10-16" @default.
• W2076012105 title "The NMR structure of the murine DLC2 SAM domain reveals a variant fold that is similar to a four-helix bundle" @default.
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• W2076012105 doi "https://doi.org/10.1186/1472-6807-7-34" @default.
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