SAND DNA-binding protein domain
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| SAND | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Solution structure of the SAND domain of the putative nuclear protein homolog (5830484a20rik) | |||||||||
| Identifiers | |||||||||
| Symbol | SAND | ||||||||
| Pfam | PF01342 | ||||||||
| InterPro | IPR000770 | ||||||||
| SCOP2 | 1h5p / SCOPe / SUPFAM | ||||||||
| |||||||||
In molecular biology, the protein domain SAND is named after a range of proteins in the protein family: Sp100, AIRE-1, NucP41/75, DEAF-1. It is localised in the cell nucleus and has an important function in chromatin-dependent transcriptional control. It is found solely in eukaryotes.
The precise function of the protein domain SAND remains to be determined. Nevertheless, it is thought to be a DNA binding domain despite its beta structure. This function can be inferred by studying the DEAF-1 transcription factor.[1] Here, the conserved positively charged residues in the SAND domains suggest the existence of negatively charged ligands. DNA is a negatively charged molecule due to the phosphate found in its backbone. Henceforth, this suggests that the SAND domain is the DNA-binding region of DEAF-1.[2]
Structure
The structure of this protein domain contains a globular fold. It is thought to have an alpha/beta secondary structure that consists of five beta strands.[2] This structure is made up of a five-stranded antiparallel beta-sheet with four alpha-helices. Further, the SAND domain is thought to have a modular structure; it can be associated with the bromodomain, the PHD finger and the MYND finger.[2]