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NRs share a modular structure, which includes highly conserved DNA- and ligand-binding domains (DBDs, LBDs) spaced by a variable hinge region [1], [2].
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A variable hinge region connects both domains.
All HP1 family members share a similar structure: an amino-terminal chromodomain (CD), a variable hinge region and a carboxy-terminal chromoshadow domain (CSD) [ 8].
The DBD links-up to the LBD by an extremely variable hinge region that contains the nuclear localization sequence and provides flexibility to NRs (1 4).
As shown, there are four major structural features found in these receptors: A signal peptide followed by a variable number of LRRs, a "hinge" region with conserved motifs at each end, and the 7TM region.
Each S100 protein monomer contains two EF-hand structures, specialized in binding calcium ions, which are linked by a central hinge region of variable length.
The two domains are separated by a hinge region of variable length, which has been related to DNA and RNA binding [ 42, 53].
The two are connected by a flexible hinge region.
These proteins consist of two globular domains with a α/β fold that are connected by a flexible hinge.
Between repeats 15 and 16, there is a hinge domain, and repeat 24 is separated from repeat 23 by a second hinge domain.
The structure reveals both 'open' and 'closed' monomer conformations, linked by a flexible hinge domain.
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