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Structure of Sox17 Bound to DNAStructure of Sox17 Bound to DNA
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSox17 regulates endodermal lineage commitment and is thought to function antagonistically to the pluripotency determinant Sox2. To investigate the biochemical basis for the distinct functions of Sox2 and Sox17, we solved the crystal structure of the high mobility group domain of Sox17 bound to a DNA element derived from the Lama1 enhancer using crystals diffracting to 2.7 A resolution. Sox17 targets the minor groove and bends the DNA by approximately 80 degrees . The DNA architecture closely resembles the one seen for Sox2/DNA structures, suggesting that the degree of bending is conserved between both proteins and nucleotide substitutions have only marginal effects on the bending topology. Accordingly, affinities of Sox2 and Sox17 for the Lama1 element were found to be identical. However, when the Oct1 contact interface of Sox2 is compared with the corresponding region of Sox17, a significantly altered charge distribution is observed, suggesting differential co-factor recruitment that may explain their biological distinctiveness. The structure of Sox17 bound to DNA reveals a conserved bending topology but selective protein interaction platforms.,Palasingam P, Jauch R, Ng CK, Kolatkar PR J Mol Biol. 2009 May 8;388(3):619-30. Epub 2009 Mar 25. PMID:19328208[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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