The ubiquitin-like domain (ULD) of about 100 amino acids is found in two
protein families:
SATB (Special AT-rich binding protein) family proteins have emerged as key
regulators that integrate higher-order chromatin organization with the
regulation of gene expression. SATB family chromatin organizers are
involved in long-range enhancer function, extension of chromatin
modifications and dynamic tethering of chromatin loops, and play diverse
and important roles in regulating the dynamic equilibrium of apoptosis,
cell invasion, metastasis, proliferation, angiogenesis, and immune
modulation. SATB family proteins consist of ULD and CUTL (see <PDOC51983>)
domains at the N terminus, a homeodomain (HD) (see <PDOC00027>) at the C
terminus, and tandem CUT domains (see <PDOC51042>) in the center
[1,2,3,4,5].
The Compass family proteins defective proventriculus (dve) from Drosophila,
required for the formation of the proventriculus and proximodistal
patterning of the wing disc, and dve-1 from Caenorhabditis elegans,
required for embryonic development and maintenance of mitochondrial
morphology. They contain the ULD domain as well as two atypical HDs
[4,5,6].
The ULD domain adopts an ubiquitin-like fold comprising four antiparallel
β-sheets that are flanked by four α-helices (see <PDB:3TUO>). The
ULD domain of SATB1 assembles into a tetramer and the tetramerization of SATB1
is essential for recognizing specific DNA sequences (such as multiple AT-rich
DNA fragments) [2,3].
The profile we developed covers the entire ULD domain.
Wang Z. Yang X. Guo S. Yang Y. Su X.-C. Shen Y. Long J.
Title
Crystal structure of the ubiquitin-like domain-CUT repeat-like tandem of special AT-rich sequence binding protein 1 (SATB1) reveals a coordinating DNA-binding mechanism.
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