Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6QNX

Structure of the SA2/SCC1/CTCF complex

Replaces:  6QNY
Summary for 6QNX
Entry DOI10.2210/pdb6qnx/pdb
DescriptorCohesin subunit SA-2, 64-kDa C-terminal product, Transcriptional repressor CTCF, ... (4 entities in total)
Functional Keywordscohesin, ctcf, tad, chromatin folding, genome regulation, sa2, gene regulation
Biological sourceHomo sapiens (human)
More
Total number of polymer chains3
Total formula weight130890.87
Authors
Li, Y.,Muir, K.W.,Panne, D. (deposition date: 2019-02-12, release date: 2020-01-22, Last modification date: 2024-10-16)
Primary citationLi, Y.,Haarhuis, J.H.I.,Sedeno Cacciatore, A.,Oldenkamp, R.,van Ruiten, M.S.,Willems, L.,Teunissen, H.,Muir, K.W.,de Wit, E.,Rowland, B.D.,Panne, D.
The structural basis for cohesin-CTCF-anchored loops.
Nature, 578:472-476, 2020
Cited by
PubMed Abstract: Cohesin catalyses the folding of the genome into loops that are anchored by CTCF. The molecular mechanism of how cohesin and CTCF structure the 3D genome has remained unclear. Here we show that a segment within the CTCF N terminus interacts with the SA2-SCC1 subunits of human cohesin. We report a crystal structure of SA2-SCC1 in complex with CTCF at a resolution of 2.7 Å, which reveals the molecular basis of the interaction. We demonstrate that this interaction is specifically required for CTCF-anchored loops and contributes to the positioning of cohesin at CTCF binding sites. A similar motif is present in a number of established and newly identified cohesin ligands, including the cohesin release factor WAPL. Our data suggest that CTCF enables the formation of chromatin loops by protecting cohesin against loop release. These results provide fundamental insights into the molecular mechanism that enables the dynamic regulation of chromatin folding by cohesin and CTCF.
PubMed: 31905366
DOI: 10.1038/s41586-019-1910-z
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

236371

PDB entries from 2025-05-21

PDB statisticsPDBj update infoContact PDBjnumon