8zys

Crystal structure of HSF5 DNA-binding domain in complex with 3-site HSE DNA (25 bp)

spinqualitylabelsall models 8zys, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8zys is a 10 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HSF5_HUMAN DNA-binding transcription factor that is essential for male fertility, spermatogenesis and meiotic prophase progression in spermatocytes under non-stress conditions. Positvely and negatively regulates gene expression to ensure progression of meiotic prophase beyond pachytene stage in spermatocytes. Plays a role in male germline meiotic sex chromosome remodeling and silencing through regulation of SMARCA4.[UniProtKB:Q5ND04] Publication Abstract from PubMed 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. Structures of heat shock factor trimers bound to DNA.,Feng N, Feng H, Wang S, Punekar AS, Ladenstein R, Wang DC, Zhang Q, Ding J, Liu W iScience. 2021 Aug 5;24(9):102951. doi: 10.1016/j.isci.2021.102951. eCollection , 2021 Sep 24. PMID:34458700 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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