1h5p

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[[Image:1h5p.jpg|left|200px]]
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{{Structure
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{{STRUCTURE_1h5p| PDB=1h5p | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h5p OCA], [http://www.ebi.ac.uk/pdbsum/1h5p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h5p RCSB]</span>
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'''SOLUTION STRUCTURE OF THE HUMAN SP100B SAND DOMAIN BY HETERONUCLEAR NMR.'''
'''SOLUTION STRUCTURE OF THE HUMAN SP100B SAND DOMAIN BY HETERONUCLEAR NMR.'''
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[[Category: Liu, Z.]]
[[Category: Liu, Z.]]
[[Category: Sattler, M.]]
[[Category: Sattler, M.]]
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[[Category: alternative splicing]]
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[[Category: Alternative splicing]]
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[[Category: antigen]]
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[[Category: Antigen]]
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[[Category: dna binding]]
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[[Category: Dna binding]]
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[[Category: kdwk]]
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[[Category: Kdwk]]
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[[Category: nmr]]
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[[Category: Nmr]]
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[[Category: nuclear protein]]
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[[Category: Nuclear protein]]
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[[Category: sand domain]]
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[[Category: Sand domain]]
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[[Category: sp100b]]
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[[Category: Sp100b]]
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[[Category: transcription]]
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[[Category: Transcription]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:27:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:58:18 2008''
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Revision as of 15:27, 2 May 2008

Image:1h5p.jpg

Template:STRUCTURE 1h5p

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 Page seeded by OCA on Fri May 2 18:27:58 2008

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