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8BFJ

CNOT11-GGNBP2 complex

Summary for 8BFJ
Entry DOI10.2210/pdb8bfj/pdb
DescriptorCCR4-NOT transcription complex subunit 11, Gametogenetin-binding protein 2, 1,2-ETHANEDIOL, ... (4 entities in total)
Functional Keywordscnot11-ggnbp2 complex, rna binding protein
Biological sourceHomo sapiens (human)
More
Total number of polymer chains2
Total formula weight25108.14
Authors
Basquin, J.,Ozgur, S.,Conti, E. (deposition date: 2022-10-26, release date: 2022-12-28, Last modification date: 2024-06-19)
Primary citationMauxion, F.,Basquin, J.,Ozgur, S.,Rame, M.,Albrecht, J.,Schafer, I.,Seraphin, B.,Conti, E.
The human CNOT1-CNOT10-CNOT11 complex forms a structural platform for protein-protein interactions.
Cell Rep, 42:111902-111902, 2023
Cited by
PubMed Abstract: The evolutionary conserved CCR4-NOT complex functions in the cytoplasm as the main mRNA deadenylase in both constitutive mRNA turnover and regulated mRNA decay pathways. The versatility of this complex is underpinned by its modular multi-subunit organization, with distinct structural modules actuating different functions. The structure and function of all modules are known, except for that of the N-terminal module. Using different structural approaches, we obtained high-resolution data revealing the architecture of the human N-terminal module composed of CNOT1, CNOT10, and CNOT11. The structure shows how two helical domains of CNOT1 sandwich CNOT10 and CNOT11, leaving the most conserved domain of CNOT11 protruding into solvent as an antenna. We discovered that GGNBP2, a protein identified as a tumor suppressor and spermatogenic factor, is a conserved interacting partner of the CNOT11 antenna domain. Structural and biochemical analyses thus pinpoint the N-terminal CNOT1-CNOT10-CNOT11 module as a conserved protein-protein interaction platform.
PubMed: 36586408
DOI: 10.1016/j.celrep.2022.111902
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.23 Å)
Structure validation

226707

건을2024-10-30부터공개중

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