Summary information and primary citation
- PDB-id
-
7vup;
DSSR-derived features in text and
JSON formats
- Class
- DNA binding protein-DNA
- Method
- X-ray (3.4 Å)
- Summary
- Structure of nf-kb p52 homodimer bound to +1--1 swap
p-selectin kb DNA fragment
- Reference
-
Pan W, Meshcheryakov VA, Li T, Wang Y, Ghosh G, Wang VY
(2023): "Structures
of NF-kappa B p52 homodimer-DNA complexes rationalize
binding mechanisms and transcription activation."
Elife, 12. doi: 10.7554/eLife.86258.
- Abstract
- The mammalian NF-κB p52:p52 homodimer together with its
cofactor Bcl3 activates transcription of κB sites with a
central G/C base pair (bp), while it is inactive toward κB
sites with a central A/T bp. To understand the molecular
basis for this unique property of p52, we have determined
the crystal structures of recombinant human p52 protein in
complex with a P-selectin(PSel)-κB DNA (5'-GGGGT
