Cys47

Cys47 refers to a specific cysteine residue located at position 47 within a protein sequence. Cysteine is an amino acid characterized by its thiol side chain (-SH). This thiol group is highly reactive and plays crucial roles in protein structure and function. It can form disulfide bonds with other cysteine residues, creating covalent linkages that stabilize protein folding. These disulfide bonds are particularly important in the extracellular environment where oxidative conditions favor their formation.

Beyond structural roles, the thiol group of cysteine can participate in catalytic mechanisms as an enzyme active site residue, acting as a nucleophile in various biochemical reactions. It can also be subject to post-translational modifications such as S-nitrosylation, S-glutathionylation, or oxidation to sulfenic acid, sulfinic acid, or sulfonic acid. These modifications can alter protein activity, localization, or interactions with other molecules.

The specific function of Cys47 is entirely dependent on the protein it is part of. Its location within the protein's three-dimensional structure, its proximity to other amino acids, and the surrounding cellular environment all contribute to its role. For instance, if Cys47 is positioned in the active site of an enzyme, it might directly participate in catalysis. If it is solvent-exposed and paired with another cysteine, it is likely involved in disulfide bond formation for structural integrity. Researchers often mutate Cys47 to other amino acids (e.g., alanine) to investigate its contribution to protein function through biochemical assays and structural studies. Understanding the properties and reactivity of Cys47 helps elucidate the overall mechanisms of the protein.