Rde 4 sandbox: Difference between revisions

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== Structure of RDE-4 ==

RDE-4 has five major regions: an N-terminal region (residues ~~1–43~~), two dsRBDs (residues 44–108 and 170–235), a long linker (residues 109–169) and a C-terminal domain (residues 236–385). Amino acid residues 1–32 and 136–151 adopt a random coiled structure and do not make any contact within itself or with the rest of the structure. Parts of the linker, residues 109–135 and 152–169, assume an α-helix and an extended loop structure, respectively. There is not any long-range nuclear Overhauser effect information between regions 1–135 and 152– 243, suggesting that the unstructured part of the linker 136–151 separates both of these regions. The region encompassed by 236–243 folds into an α-helix. The amino acid regions 44–108 and 170–235 form dsRBD1 and dsRBD2, respectively. The hydrophobic residues Leu45, Val47, Leu48, Val55, Trp62, Met73, Leu75, Leu77, Ile80, Val82, Leu101, and Val105 stabilize dsRBD1, and Val171, Leu174, Leu183, Val201, Met205, Met227, and Leu232 form the core of dsRBD2. Apart from the canonical dsRBD fold, there are additional secondary-structural elements that are observed in both RDE-4D1 and RDE-4D2. <ref name=second>DOI:DOI: 10.1042/BJ20131347</ref> (Purple citation)

RDE-4 has five major regions: an <scene name='79/798389/N-terminal_of_rde-4/1'>N-terminal region (residues 1-43)</scene>, two dsRBDs (residues 44–108 and 170–235), a long linker (residues 109–169) and a C-terminal domain (residues 236–385). Amino acid residues 1–32 and 136–151 adopt a random coiled structure and do not make any contact within itself or with the rest of the structure. Parts of the linker, residues 109–135 and 152–169, assume an α-helix and an extended loop structure, respectively. There is not any long-range nuclear Overhauser effect information between regions 1–135 and 152– 243, suggesting that the unstructured part of the linker 136–151 separates both of these regions. The region encompassed by 236–243 folds into an α-helix. The amino acid regions 44–108 and 170–235 form dsRBD1 and dsRBD2, respectively. The hydrophobic residues Leu45, Val47, Leu48, Val55, Trp62, Met73, Leu75, Leu77, Ile80, Val82, Leu101, and Val105 stabilize dsRBD1, and Val171, Leu174, Leu183, Val201, Met205, Met227, and Leu232 form the core of dsRBD2. Apart from the canonical dsRBD fold, there are additional secondary-structural elements that are observed in both RDE-4D1 and RDE-4D2. <ref name=second>DOI:DOI: 10.1042/BJ20131347</ref> (Purple citation)

== Function ==

Rde 4 sandbox: Difference between revisions

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 == Structure of RDE-4 ==
-RDE-4 has five major regions: an N-terminal region (residues 1–43), two dsRBDs (residues 44–108 and 170–235), a long linker (residues 109–169) and a C-terminal domain (residues 236–385). Amino acid residues 1–32 and 136–151 adopt a random coiled structure and do not make any contact within itself or with the rest of the structure. Parts of the linker, residues 109–135 and 152–169, assume an α-helix and an extended loop structure, respectively. There is not any long-range nuclear Overhauser effect information between regions 1–135 and 152– 243, suggesting that the unstructured part of the linker 136–151 separates both of these regions. The region encompassed by 236–243 folds into an α-helix. The amino acid regions 44–108 and 170–235 form dsRBD1 and dsRBD2, respectively. The hydrophobic residues Leu45, Val47, Leu48, Val55, Trp62, Met73, Leu75, Leu77, Ile80, Val82, Leu101, and Val105 stabilize dsRBD1, and Val171, Leu174, Leu183, Val201, Met205, Met227, and Leu232 form the core of dsRBD2. Apart from the canonical dsRBD fold, there are additional secondary-structural elements that are observed in both RDE-4D1 and RDE-4D2. <ref name=second>DOI:DOI: 10.1042/BJ20131347</ref> (Purple citation)
+RDE-4 has five major regions: an <scene name='79/798389/N-terminal_of_rde-4/1'>N-terminal region (residues 1-43)</scene>, two dsRBDs (residues 44–108 and 170–235), a long linker (residues 109–169) and a C-terminal domain (residues 236–385). Amino acid residues 1–32 and 136–151 adopt a random coiled structure and do not make any contact within itself or with the rest of the structure. Parts of the linker, residues 109–135 and 152–169, assume an α-helix and an extended loop structure, respectively. There is not any long-range nuclear Overhauser effect information between regions 1–135 and 152– 243, suggesting that the unstructured part of the linker 136–151 separates both of these regions. The region encompassed by 236–243 folds into an α-helix. The amino acid regions 44–108 and 170–235 form dsRBD1 and dsRBD2, respectively. The hydrophobic residues Leu45, Val47, Leu48, Val55, Trp62, Met73, Leu75, Leu77, Ile80, Val82, Leu101, and Val105 stabilize dsRBD1, and Val171, Leu174, Leu183, Val201, Met205, Met227, and Leu232 form the core of dsRBD2. Apart from the canonical dsRBD fold, there are additional secondary-structural elements that are observed in both RDE-4D1 and RDE-4D2. <ref name=second>DOI:DOI: 10.1042/BJ20131347</ref> (Purple citation)
 == Function ==