1C8Z
C-TERMINAL DOMAIN OF MOUSE BRAIN TUBBY PROTEIN
Summary for 1C8Z
| Entry DOI | 10.2210/pdb1c8z/pdb |
| Descriptor | TUBBY PROTEIN, PHOSPHATE ION (3 entities in total) |
| Functional Keywords | tubby filled-barrel, beta-barrel, filled-beta-roll, 12-stranded-beta-barrel, helix-filled-barrel, obesity blindness, deafness, signaling protein |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 30186.15 |
| Authors | Boggon, T.J.,Myers, S.C.,Shapiro, L. (deposition date: 1999-07-30, release date: 1999-12-12, Last modification date: 2024-02-07) |
| Primary citation | Boggon, T.J.,Shan, W.S.,Santagata, S.,Myers, S.C.,Shapiro, L. Implication of tubby proteins as transcription factors by structure-based functional analysis. Science, 286:2119-2125, 1999 Cited by PubMed Abstract: Tubby-like proteins (TULPs) are found in a broad range of multicellular organisms. In mammals, genetic mutation of tubby or other TULPs can result in one or more of three disease phenotypes: obesity (from which the name "tubby" is derived), retinal degeneration, and hearing loss. These disease phenotypes indicate a vital role for tubby proteins; however, no biochemical function has yet been ascribed to any member of this protein family. A structure-directed approach was employed to investigate the biological function of these proteins. The crystal structure of the core domain from mouse tubby was determined at a resolution of 1.9 angstroms. From primarily structural clues, experiments were devised, the results of which suggest that TULPs are a unique family of bipartite transcription factors. PubMed: 10591637DOI: 10.1126/science.286.5447.2119 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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