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Despite immense diversity within the recognized substrates, all members of the family share a common fold that includes two domains that are separated by a conserved hinge.
These two domains are connected by a conserved hinge region which allows the conformational change of the complex structure bringing the two ligands into close proximity during catalysis (Bernstein et al., 1997).
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Two hydrophobic patches are noted on either side of the conserved hinge segment.
For the L1 protein, there are two domains separated by a conserved and flexible hinge region made of Gly67, Gly69, and Gly159.
In general, it should be more frequent for non-inhibitory serpin-fold to evolve from an active inhibitor than the reverse; a single substitution within the conserved hinge-region motif can inactivate the inhibitory mechanism [ 4]; while a series of changes in a non-inhibitory serpin-fold would be required to generate the hinge-region consensus.
The substrate is activated through protonation by a conserved tyrosine.
Comparison of cryo-EM structures of virus E proteins to rE crystal structures showed that the E proteins on the virus had a conserved DI-DII hinge angle, whereas the hinge angle on the rE proteins is highly variable.
The MthK channel has splayed bent helices rather than the tepee shape, and it has been postulated(10) that pore gating involves a molecular hinge about a conserved glycine residue.
We also detected that the putative hinge also comprises a conserved (100%) aromatic phenylalanine (F), aliphatic alanine (A) and leucines (L).
Predicted highly conserved α-helices are connected by the less conserved hinge regions (Budanov et al, 2002).
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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