2COM: The solution structure of the SWIRM domain of human LSD1

SWIRM is an evolutionarily conserved domain involved in several chromatin-modifying complexes. Recently, the LSD1 protein, which bears a SWIRM domain, was found to be a demethylase for Lys4-methylated histone H3. Here, we report a solution structure of the SWIRM domain of human LSD1. It forms a compact fold composed of 6 alpha helices, in which a 20 amino acid long helix (alpha4) is surrounded by 5 other short helices. The SWIRM domain structure could be divided into the N-terminal part (alpha1-alpha3) and the C-terminal part (alpha4-alpha6), which are connected to each other by a salt bridge. While the N-terminal part forms a SWIRM-specific structure, the C-terminal part adopts a helix-turn-helix (HTH)-related fold. We discuss a model in which the SWIRM domain acts as an anchor site for a histone tail.
PDB ID: 2COMDownload
MMDB ID: 36290
PDB Deposition Date: 2005/5/18
Updated in MMDB: 2005/12
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Molecular Components in 2COM
Label Count Molecule
Protein (1 molecule)
Lysine-specific Histone Demethylase 1(Gene symbol: KDM1A)
Molecule annotation
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