5d8k

Human HSF2 DNA-Binding Domain bound to 2-site HSE DNA at 1.73 Angstroms Resolution

spinqualitylabelsall models 5d8k, resolution 1.73Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5d8k is a 2 chain structure with sequence from Homo sapiens and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HSF2_HUMAN DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked. Publication Abstract from PubMed Heat-shock transcription factor (HSF) family members function in stress protection and in human diseases including proteopathies, neurodegeneration and cancer. The mechanisms that drive distinct post-translational modifications, cofactor recruitment and target-gene activation for specific HSF paralogs are unknown. We present crystal structures of the human HSF2 DNA-binding domain (DBD) bound to DNA, revealing an unprecedented view of HSFs that provides insights into their unique biology. The HSF2 DBD structures resolve a new C-terminal helix that directs wrapping of the coiled-coil domain around DNA, thereby exposing paralog-specific sequences of the DBD surface for differential post-translational modifications and cofactor interactions. We further demonstrate a direct interaction between HSF1 and HSF2 through their coiled-coil domains. Together, these features provide a new model for HSF structure as the basis for differential and combinatorial regulation, which influences the transcriptional response to cellular stress. Structures of HSF2 reveal mechanisms for differential regulation of human heat-shock factors.,Jaeger AM, Pemble CW 4th, Sistonen L, Thiele DJ Nat Struct Mol Biol. 2016 Jan 4. doi: 10.1038/nsmb.3150. PMID:26727490 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Heat shock factor

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