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4A3N

Crystal Structure of HMG-BOX of Human SOX17

Summary for 4A3N
Entry DOI10.2210/pdb4a3n/pdb
DescriptorTRANSCRIPTION FACTOR SOX-17, ZINC ION (3 entities in total)
Functional Keywordstranscription
Biological sourceHOMO SAPIENS (HUMAN)
Cellular locationNucleus (By similarity): Q9H6I2
Total number of polymer chains1
Total formula weight8641.99
Authors
Gao, N.,Gao, H.,Qian, H.,Si, S.,Xie, Y. (deposition date: 2011-10-01, release date: 2011-12-28, Last modification date: 2023-12-20)
Primary citationGao, N.,Jiang, W.,Gao, H.,Cheng, Z.,Qian, H.,Si, S.,Xie, Y.
Structural Basis of Human Transcription Factor Sry-Related Box 17 Binding to DNA.
Protein Pept.Lett., 20:481-, 2013
Cited by
PubMed Abstract: Sry-related box (Sox) transcription factors share a conserved high-mobility-group box domain (HMG-domain) that binds DNA in the minor groove and bends DNA for further assembly of transcriptional machineries. During organogenesis, each member of the Sox family triggers a specific cell lineage differentiation, indicating that their interactions with DNA are different from each other. Therefore, investigating structural rearrangement of each Sox transcription factor HMG-domain upon binding to DNA would help to elucidate the distinctive molecular mechanism by which they interact with DNA. Previous studies have determined the crystal structures of Sox2 HMG-domain/DNA, Sox4 HMGdomain/ DNA, Sox9 HMG-domain/DNA and Sox17 HMG-domain/DNA complexes. However, major gaps remain in the structural information on the Sox transcription factor HMG-domains. Here, we report the crystal structure of the human Sox17 HMG-domain alone at 2.4 A resolution. Comparing this structure and the structure of the mouse Sox17 HMGdomain/ DNA complex provides structural understanding of the mechanism of Sox17 binding to DNA. Specifically, after electrostatic interactions attract Sox17 to DNA, Asn73, Ser99, and Trp106 form hydrogen bonds with DNA, Arg70, Lys80, Arg83, His94, and Asn95 on Sox17 undergo conformational changes and form hydrogen bonds with DNA, contributing to the electrostatic interaction between Sox17 and DNA.
PubMed: 23061670
DOI: 10.2174/092986613805290336
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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