Extracellular protein disulfide bonds

Extracellular protein disulfide bonds are covalent bridges formed between pairs of cysteine residues within or between polypeptide chains, predominantly in proteins secreted or located at the cell surface. These bonds stabilize protein structure, protect against extracellular proteolysis and oxidation, and enable dynamic regulation of protein conformation and function in response to changes in redox milieu. Enzymes like protein disulfide isomerase (PDI) catalyze their formation and rearrangement, processes which are essential to proper protein folding, activity modulation (e.g., integrin activation, viral entry), and cellular response to oxidative stress. Dysregulation of disulfide bond formation or cleavage is implicated in cancers, neurodegenerative diseases, thrombosis, and infections such as HIV. However, "extracellular protein disulfide bonds" describes a structural motif, not a druggable target, and should be contextualized within the specific proteins containing these bonds[1][2][4][5][6][7].

Other names

Disulfide bridgesS-S bondsProtein disulfide bonds

Inhibition of thiol isomerases (e.g., PDI) modifies extracellular disulfide exchange and alters cell surface protein functions. Redox modulation for functional regulation of target proteins.