5VJX
Crystal structure of the CLOCK Transcription Domain Exon19 in Complex with a Repressor
Summary for 5VJX
| Entry DOI | 10.2210/pdb5vjx/pdb |
| Descriptor | CLOCK-interacting pacemaker, Circadian locomoter output cycles protein kaput (3 entities in total) |
| Functional Keywords | circadian rhythm, clock protein, transcription activation, repressor, coiled coil, cipc, circadian clock, transferase |
| Biological source | Mus musculus (Mouse) More |
| Total number of polymer chains | 30 |
| Total formula weight | 195979.15 |
| Authors | Hou, Z.,Su, L.,Pei, J.,Grishin, N.V.,Zhang, H. (deposition date: 2017-04-20, release date: 2017-12-06, Last modification date: 2024-11-13) |
| Primary citation | Hou, Z.,Su, L.,Pei, J.,Grishin, N.V.,Zhang, H. Crystal Structure of the CLOCK Transactivation Domain Exon19 in Complex with a Repressor. Structure, 25:1187-1194.e3, 2017 Cited by PubMed Abstract: In the canonical clock model, CLOCK:BMAL1-mediated transcriptional activation is feedback regulated by its repressors CRY and PER and, in association with other coregulators, ultimately generates oscillatory gene expression patterns. How CLOCK:BMAL1 interacts with coregulator(s) is not well understood. Here we report the crystal structures of the mouse CLOCK transactivating domain Exon19 in complex with CIPC, a potent circadian repressor that functions independently of CRY and PER. The Exon19:CIPC complex adopts a three-helical coiled-coil bundle conformation containing two Exon19 helices and one CIPC. Unique to Exon19:CIPC, three highly conserved polar residues, Asn341 of CIPC and Gln544 of the two Exon19 helices, are located at the mid-section of the coiled-coil bundle interior and form hydrogen bonds with each other. Combining results from protein database search, sequence analysis, and mutagenesis studies, we discovered for the first time that CLOCK Exon19:CIPC interaction is a conserved transcription regulatory mechanism among mammals, fish, flies, and other invertebrates. PubMed: 28669630DOI: 10.1016/j.str.2017.05.023 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.695 Å) |
Structure validation
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