Summary for 1M8Z
| Entry DOI | 10.2210/pdb1m8z/pdb |
| Related | 1ib2 1ib3 |
| Descriptor | PUMILIO 1, BETA-MERCAPTOETHANOL (3 entities in total) |
| Functional Keywords | pumilio homology domain, puf domain, rna binding protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm (Probable): Q14671 |
| Total number of polymer chains | 1 |
| Total formula weight | 40442.66 |
| Authors | Wang, X.,Zamore, P.D.,Hall, T.M.T. (deposition date: 2002-07-26, release date: 2002-09-04, Last modification date: 2024-02-14) |
| Primary citation | Wang, X.,Zamore, P.D.,Hall, T.M. Crystal structure of a Pumilio homology domain. Mol.Cell, 7:855-865, 2001 Cited by PubMed Abstract: Puf proteins regulate translation and mRNA stability by binding sequences in their target RNAs through the Pumilio homology domain (PUM-HD), which is characterized by eight tandem copies of a 36 amino acid motif, the PUM repeat. We have solved the structure of the PUM-HD from human Pumilio1 at 1.9 A resolution. The structure reveals that the eight PUM repeats correspond to eight copies of a single, repeated structural motif. The PUM repeats pack together to form a right-handed superhelix that approximates a half doughnut. The distribution of side chains on the inner and outer faces of this half doughnut suggests that the inner face of the PUM-HD binds RNA while the outer face interacts with proteins such as Nanos, Brain Tumor, and cytoplasmic polyadenylation element binding protein. PubMed: 11336708DOI: 10.1016/S1097-2765(01)00229-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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