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8JJ6

Structure of the NELF-BCE complex

Summary for 8JJ6
Entry DOI10.2210/pdb8jj6/pdb
DescriptorNegative elongation factor B, Negative elongation factor complex member C/D, NELF-E, ... (4 entities in total)
Functional Keywordstranscription elongation factor, negative transcription elongation factor(nelf), transcription
Biological sourceHomo sapiens (human)
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Total number of polymer chains6
Total formula weight172885.60
Authors
Wang, Z.,Cao, Y.,Qin, Y. (deposition date: 2023-05-29, release date: 2023-08-30, Last modification date: 2024-09-11)
Primary citationCao, Y.,Qin, Y.,Zhang, W.,Tian, W.,Ren, Y.,Ren, J.,Wang, J.,Wang, M.,Jiang, J.,Wang, Z.
Structural basis of the human negative elongation factor NELF-B/C/E ternary complex.
Biochem.Biophys.Res.Commun., 677:155-161, 2023
Cited by
PubMed Abstract: Negative elongation factor (NELF) is a four-subunit transcription elongation factor that mainly functions in maintaining the paused state of RNA polymerase II in eukaryotes. Upon binding to Pol II, NELF works synergistically with DRB sensitivity-inducing factor (DSIF) and inhibits transcription elongation of Pol II, which subsequently retains a stably paused state 20-60 base pairs downstream of the promoter. The promoter-proximal pausing of Pol II caused by NELF is a general mechanism of transcriptional regulation for most signal-responsive genes. To date, structural studies have significantly advanced our understanding of the molecular mechanisms of NELF. However, a high quality structural model clarifying the interaction details of this complex is still lacking. In this study, we solved the high resolution crystal structure of the NELF-B/C/E ternary complex. We observed detailed interactions between subunits and identified residues important for the association between NELF-B and NELF-E. Our work presents a precise model of the NELF complex, which will facilitate our understanding of its in vivo function.
PubMed: 37591184
DOI: 10.1016/j.bbrc.2023.08.019
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.72 Å)
Structure validation

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