1h5p

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Revision as of 15:06, 12 November 2007

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SOLUTION STRUCTURE OF THE HUMAN SP100B SAND DOMAIN BY HETERONUCLEAR NMR.

Overview

The SAND domain is a conserved sequence motif found in a number of nuclear, proteins, including the Sp100 family and NUDR. These are thought to play, important roles in chromatin-dependent transcriptional regulation and are, linked to many diseases. We have determined the three-dimensional (3D), structure of the SAND domain from Sp100b. The structure represents a novel, alpha/beta fold, in which a conserved KDWK sequence motif is found within, an alpha-helical, positively charged surface patch. For NUDR, the SAND, domain is shown to be sufficient to mediate DNA binding. Using mutational, analyses and chemical shift perturbation experiments, the DNA binding, surface is mapped to the alpha-helical region encompassing the KDWK motif., The DNA binding activity of wild type and mutant proteins in vitro, correlates with transcriptional regulation activity of full length NUDR in, vivo. The evolutionarily conserved SAND domain defines a new DNA binding, fold that is involved in chromatin-associated transcriptional regulation.

About this Structure

1H5P is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The SAND domain structure defines a novel DNA-binding fold in transcriptional regulation., Bottomley MJ, Collard MW, Huggenvik JI, Liu Z, Gibson TJ, Sattler M, Nat Struct Biol. 2001 Jul;8(7):626-33. PMID:11427895

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