Summary information and primary citation
- PDB-id
-
7dcu;
DSSR-derived features in text and
JSON formats
- Class
- DNA binding protein-DNA
- Method
- X-ray (1.75 Å)
- Summary
- Crystal structure of hsf2 DNA-binding domain in complex
with 3-site hse DNA (21 bp)
- Reference
-
Feng N, Feng H, Wang S, Punekar AS, Ladenstein R, Wang
DC, Zhang Q, Ding J, Liu W (2021): "Structures
of heat shock factor trimers bound to DNA."
Iscience, 24, 102951. doi:
10.1016/j.isci.2021.102951.
- Abstract
- Heat shock factor 1 (HSF1) and 2 (HSF2) play distinct
but overlapping regulatory roles in maintaining cellular
proteostasis or mediating cell differentiation and
development. Upon activation, both HSFs trimerize and bind
to heat shock elements (HSEs) present in the promoter
region of target genes. Despite structural insights gained
from recent studies, structures reflecting the
physiological architecture of this transcriptional
machinery remains to be determined. Here, we present
co-crystal structures of human HSF1 and HSF2 trimers bound
to DNA, which reveal a triangular arrangement of the three
DNA-binding domains (DBDs) with protein-protein
interactions largely mediated by the wing domain. Two
structural properties, different flexibility of the wing
domain and local DNA conformational changes induced by HSF
binding, seem likely to contribute to the subtle
differential specificity between HSF1 and HSF2. Besides,
two more structures showing DBDs bound to "two-site"
head-to-head HSEs were determined as additions to the
published tail-to-tail dimer-binding structures.
