All TIMPs contain twelve conserved cystein residues, which form six disulfide bonds.
2.
Iron atom in the cluster is additionally bound by three other Cystein ligands :.
3.
The taste-modifying protein, miraculin, has seven cystein residues in a molecule composed of 191 amino acid residues.
4.
Low resolution studies shows that STC1 is an anti-parallel homodimer in solution and the cystein 202 is responsible for the dimerization of this protein.
5.
Structurally, it is composed of three distinct regions : an N-terminal protein domain, a hinge region and a C-terminal cystein-rich domain.
6.
Formation of a disulfide bond between two cystein residues within the protein closes the hydrophobic funnel of the catalyic site, and thus acts as an on / off switch for catalytic activity.
7.
The histidine molecule is protonated by the cysteine residue and this allows the cystein residue to undergo a nucleophillic attack on the isopeptide bond, which removes the ubiquitin from the substrate protein.
8.
The intermediate then spontaneously reacts with glutathione to form 2-L-cystein-S-yl-1, 4-dihydroxy-cyclohex-5-en-1-yl acetic acid ( hawkinsin ).
9.
In general, the structure of ROCK proteins consists of an N-terminal kinase domain, a coiled-coiled region and a PH domain containing a cystein-rich domain ( CRD ) at the C-terminal.
10.
Moreover, regucalcin has been shown to have an inhibitory effect on aminoacyl t-RNA synthetase, a rate limiting enzyme at translational process of protein synthesis and an activatory effect on cystein protease and superoxide dismutase in liver and kidney cells.
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