2D5R
Crystal Structure of a Tob-hCaf1 Complex
Summary for 2D5R
| Entry DOI | 10.2210/pdb2d5r/pdb |
| Descriptor | CCR4-NOT transcription complex subunit 7, Tob1 protein (3 entities in total) |
| Functional Keywords | poly(a) deadenylase, antiproliferative protein, transcription |
| Biological source | Homo sapiens (human) More |
| Cellular location | Nucleus: Q9UIV1 |
| Total number of polymer chains | 2 |
| Total formula weight | 42930.09 |
| Authors | Horiuchi, M.,Suzuki, N.N.,Muroya, N.,Takahasi, K.,Nishida, M.,Yoshida, Y.,Ikematsu, N.,Nakamura, T.,Kawamura-Tsuzuku, J.,Yamamoto, T.,Inagaki, F. (deposition date: 2005-11-04, release date: 2006-12-12, Last modification date: 2024-03-13) |
| Primary citation | Horiuchi, M.,Takeuchi, K.,Noda, N.,Muroya, N.,Suzuki, T.,Nakamura, T.,Kawamura-Tsuzuku, J.,Takahasi, K.,Yamamoto, T.,Inagaki, F. Structural basis for the antiproliferative activity of the Tob-hCaf1 complex. J.Biol.Chem., 284:13244-13255, 2009 Cited by PubMed Abstract: The Tob/BTG family is a group of antiproliferative proteins containing two highly homologous regions, Box A and Box B. These proteins all associate with CCR4-associated factor 1 (Caf1), which belongs to the ribonuclease D (RNase D) family of deadenylases and is a component of the CCR4-Not deadenylase complex. Here we determined the crystal structure of the complex of the N-terminal region of Tob and human Caf1 (hCaf1). Tob exhibited a novel fold, whereas hCaf1 most closely resembled the catalytic domain of yeast Pop2 and human poly(A)-specific ribonuclease. Interestingly, the association of hCaf1 was mediated by both Box A and Box B of Tob. Cell growth assays using both wild-type and mutant proteins revealed that deadenylase activity of Caf1 is not critical but complex formation is crucial to cell growth inhibition. Caf1 tethers Tob to the CCR4-Not deadenylase complex, and thereby Tob gathers several factors at its C-terminal region, such as poly(A)-binding proteins, to exert antiproliferative activity. PubMed: 19276069DOI: 10.1074/jbc.M809250200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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