1hdp
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(New page: 200px<br /> <applet load="1hdp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hdp" /> '''SOLUTION STRUCTURE OF A POU-SPECIFIC HOMEOD...)
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Revision as of 15:10, 12 November 2007
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SOLUTION STRUCTURE OF A POU-SPECIFIC HOMEODOMAIN: 3D-NMR STUDIES OF HUMAN B-CELL TRANSCRIPTION FACTOR OCT-2
Overview
The POU DNA-binding motif defines a conserved family of eukaryotic, transcription factors involved in regulation of gene expression. This, bipartite motif consists of an N-terminal POU-specific domain (POUs), a, flexible linker, and a C-terminal POU-specific homeodomain (POUHD). Here, we describe the solution structure of a POU-specific homeodomain. An NMR, model is obtained from Oct-2, a human B-cell specific transcription factor, which participates in the regulation of immunoglobulin genes. A fragment, of Oct-2 containing POUHD and an adjoining linker was expressed in, Escherichia coli and characterized by three-dimensional nuclear magnetic, resonance (3D-NMR) spectroscopy. Complete 1H and 15N resonance assignment, of the POUHD moiety is presented. The POUHD solution structure, as, calculated by distance geometry and simulated annealing (DG/SA), is, similar to that of canonical homeodomains. A salient difference between, solution and crystal structures is observed in the C-terminal segment of, alpha-helix 3 (the HTH recognition helix), which is not well ordered in, solution. Because this segment presumably folds upon specific DNA binding, its flexibility in solution may reduce the intrinsic DNA affinity of POUHD, in the absence of POUs.
About this Structure
1HDP is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of a POU-specific homeodomain: 3D-NMR studies of human B-cell transcription factor Oct-2., Sivaraja M, Botfield MC, Mueller M, Jancso A, Weiss MA, Biochemistry. 1994 Aug 23;33(33):9845-55. PMID:7914745
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