2uy1: Difference between revisions

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==Overview==

The cleavage stimulation factor (CstF) is essential for the first step of, poly(A) tail formation at the 3' ends of mRNAs. This heterotrimeric, complex is built around the 77-kDa protein bridging both CstF-64 and, CstF-50 subunits. We have solved the crystal structure of the 77-kDa, protein from Encephalitozoon cuniculi at a resolution of 2 A. The, structure folds around 11 Half-a-TPR repeats defining two domains. The, crystal structure reveals a tight homodimer exposing phylogenetically, conserved areas for interaction with protein partners. Mapping experiments, identify the C-terminal region of Rna14p, the yeast counterpart of, CstF-77, as the docking domain for Rna15p, the yeast CstF-64 homologue.

The cleavage stimulation factor (CstF) is essential for the first step of poly(A) tail formation at the 3' ends of mRNAs. This heterotrimeric complex is built around the 77-kDa protein bridging both CstF-64 and CstF-50 subunits. We have solved the crystal structure of the 77-kDa protein from Encephalitozoon cuniculi at a resolution of 2 A. The structure folds around 11 Half-a-TPR repeats defining two domains. The crystal structure reveals a tight homodimer exposing phylogenetically conserved areas for interaction with protein partners. Mapping experiments identify the C-terminal region of Rna14p, the yeast counterpart of CstF-77, as the docking domain for Rna15p, the yeast CstF-64 homologue.

==About this Structure==

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[[Category: rna-binding protein]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-The cleavage stimulation factor (CstF) is essential for the first step of, poly(A) tail formation at the 3' ends of mRNAs. This heterotrimeric, complex is built around the 77-kDa protein bridging both CstF-64 and, CstF-50 subunits. We have solved the crystal structure of the 77-kDa, protein from Encephalitozoon cuniculi at a resolution of 2 A. The, structure folds around 11 Half-a-TPR repeats defining two domains. The, crystal structure reveals a tight homodimer exposing phylogenetically, conserved areas for interaction with protein partners. Mapping experiments, identify the C-terminal region of Rna14p, the yeast counterpart of, CstF-77, as the docking domain for Rna15p, the yeast CstF-64 homologue.
+The cleavage stimulation factor (CstF) is essential for the first step of poly(A) tail formation at the 3' ends of mRNAs. This heterotrimeric complex is built around the 77-kDa protein bridging both CstF-64 and CstF-50 subunits. We have solved the crystal structure of the 77-kDa protein from Encephalitozoon cuniculi at a resolution of 2 A. The structure folds around 11 Half-a-TPR repeats defining two domains. The crystal structure reveals a tight homodimer exposing phylogenetically conserved areas for interaction with protein partners. Mapping experiments identify the C-terminal region of Rna14p, the yeast counterpart of CstF-77, as the docking domain for Rna15p, the yeast CstF-64 homologue.
 ==About this Structure==
@@ Line 19: / Line 19: @@
 [[Category: rna-binding protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:41:53 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:51:31 2008''