1xbr | pdb_00001xbr

T DOMAIN FROM XENOPUS LAEVIS BOUND TO DNA

spinqualitylabelsall models 1xbr, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1xbr is a 4 chain structure with sequence from Xenopus laevis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: XBRA (Xenopus laevis) Resources: FirstGlance, OCA, RCSB, PDBsum Function [BRAC_XENLA] Involved in the transcriptional regulation of genes required for mesoderm formation and differentiation. Causes dorsal mesodermal differentiation of animal cap ectoderm when co-expressed with wnt8 and noggin. None of these molecules causes dorsal mesoderm formation when expressed alone. Establishes the left/right axis at early gastrula stage by directly up-regulating mesodermal expression of zic3. 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 PubMed The mouse Brachyury (T) gene is the prototype of a growing family of so-called T-box genes which encode transcriptional regulators and have been identified in a variety of invertebrates and vertebrates, including humans. Mutations in Brachyury and other T-box genes result in drastic embryonic phenotypes, indicating that T-box gene products are essential in tissue specification, morphogenesis and organogenesis. The T-box encodes a DNA-binding domain of about 180 amino-acid residues, the T domain. Here we report the X-ray structure of the T domain from Xenopus laevis in complex with a 24-nucleotide palindromic DNA duplex. We show that the protein is bound as a dimer, interacting with the major and the minor grooves of the DNA. A new type of specific DNA contact is seen, in which a carboxy-terminal helix is deeply embedded into an enlarged minor groove without bending the DNA. Hydrophobic interactions and an unusual main-chain carbonyl contact to a guanine account for sequence-specific recognition in the minor groove by this helix. Thus the structure of this T domain complex with DNA reveals a new way in which a protein can recognize DNA. Crystallographic structure of the T domain-DNA complex of the Brachyury transcription factor.,Muller CW, Herrmann BG Nature. 1997 Oct 23;389(6653):884-8. PMID:9349824 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Brachyury

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