2r5y

Structure of Scr/Exd complex bound to a consensus Hox-Exd site

spinqualitylabelsall models 2r5y, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2r5y is a 4 chain structure with sequence from Drosophila melanogaster and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.6Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SCR_DROME Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Controls the segmental transformation of the first to the second thoracic segment (prothorax to mesothorax) and of the labial palps into maxillary palps. In embryo, required for fusion of labial lobes and development of the T1 denticle belt. In adult, expression in the head is necessary for proper development of the labium. In the first thoracic segment of the adult, required for proper development of the sex comb and to suppress improper prothoracic wing development. 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 recognition of specific DNA-binding sites by transcription factors is a critical yet poorly understood step in the control of gene expression. Members of the Hox family of transcription factors bind DNA by making nearly identical major groove contacts via the recognition helices of their homeodomains. In vivo specificity, however, often depends on extended and unstructured regions that link Hox homeodomains to a DNA-bound cofactor, Extradenticle (Exd). Using a combination of structure determination, computational analysis, and in vitro and in vivo assays, we show that Hox proteins recognize specific Hox-Exd binding sites via residues located in these extended regions that insert into the minor groove but only when presented with the correct DNA sequence. Our results suggest that these residues, which are conserved in a paralog-specific manner, confer specificity by recognizing a sequence-dependent DNA structure instead of directly reading a specific DNA sequence. Functional specificity of a Hox protein mediated by the recognition of minor groove structure.,Joshi R, Passner JM, Rohs R, Jain R, Sosinsky A, Crickmore MA, Jacob V, Aggarwal AK, Honig B, Mann RS Cell. 2007 Nov 2;131(3):530-43. PMID:17981120 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Hox protein

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