5DV2
Crystal structure of human CNOT6L in complex with cytidine-5'-monophosphate
Summary for 5DV2
| Entry DOI | 10.2210/pdb5dv2/pdb |
| Related | 5DV4 |
| Descriptor | CCR4-NOT transcription complex subunit 6-like, CYTIDINE-5'-MONOPHOSPHATE (3 entities in total) |
| Functional Keywords | nuclease domain, deadenylase, inhibitor complex, hydrolase |
| Biological source | Homo sapiens (Human) |
| Cellular location | Cytoplasm: Q96LI5 |
| Total number of polymer chains | 1 |
| Total formula weight | 45463.70 |
| Authors | Zhang, Q.,Bartlam, M. (deposition date: 2015-09-21, release date: 2016-05-18, Last modification date: 2024-03-20) |
| Primary citation | Zhang, Q.,Yan, D.,Guo, E.,Ding, B.,Yang, W.,Liu, R.,Yamamoto, T.,Bartlam, M. Structural basis for inhibition of the deadenylase activity of human CNOT6L Febs Lett., 590:1270-1279, 2016 Cited by PubMed Abstract: Human CNOT6L/CCR4, a member of the endonuclease-exonuclease-phosphatase (EEP) family enzymes, is one of the two deadenylase enzymes in the conserved CCR4-NOT complex. Here, we report inhibitor-bound crystal structures of the human CNOT6L nuclease domain in complex with the nucleotide CMP and the aminoglycoside neomycin. Deadenylase activity assays show that nucleotides are effective inhibitors of both CNOT6L and CNOT7, with AMP more effective than other nucleotides, and that neomycin is a weak deadenylase inhibitor. Structural analysis shows that all inhibitors occupy the substrate and magnesium-binding sites of CNOT6L, suggesting that inhibitors compete with both substrate and divalent magnesium ions for overlapping binding sites. PubMed: 27013054DOI: 10.1002/1873-3468.12160 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.07 Å) |
Structure validation
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