1H5P

Solution structure of the human Sp100b SAND domain by heteronuclear NMR.

Summary for 1H5P

• Entry DOI: 10.2210/pdb1h5p/pdb
• NMR Information: BMRB: 5558
• Descriptor: NUCLEAR AUTOANTIGEN SP100-B (1 entity in total)
• Functional Keywords: transcription, dna binding, sp100b, sand domain, kdwk, antigen, nuclear protein, alternative splicing
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Nucleus. Isoform Sp100-C: Nucleus : P23497
• Total number of polymer chains: 1
• Total formula weight: 11052.81

Authors

Bottomley, M.J.,Liu, Z.,Collard, M.W.,Huggenvik, J.I.,Gibson, T.J.,Sattler, M. (deposition date: 2001-05-24, release date: 2001-07-06, Last modification date: 2024-05-15)

Primary citation

Bottomley, M.J.,Collard, M.W.,Huggenvik, J.I.,Liu, Z.,Gibson, T.J.,Sattler, M.
The SAND domain structure defines a novel DNA-binding fold in transcriptional regulation.
Nat. Struct. Biol., 8:626-633, 2001

PubMed Abstract: 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.

PubMed: 11427895
DOI: 10.1038/89675

Experimental method

SOLUTION NMR