Journal
CURRENT PROTEIN & PEPTIDE SCIENCE
Volume 8, Issue 5, Pages 484-495Publisher
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/138920307782411464
Keywords
redox-active disulfide; redox signaling; cross-strand disulfide; cytokine receptor; major histocompatibility complex
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Seminal studies by Richardson [11 and Thornton [2] defined the constraints imposed by protein structure on disulfide formation and flagged forbidden regions of primary or secondary structure seemingly incapable of forming disulfide bonds between resident cysteine pairs. With respect to secondary structure, disulfide bonds were not found between cysteine pairs: A. on adjacent beta-stands [1]; B. in a single helix or strand [2]; C. on non-adjacent strands of the same beta-sheet [2]. In primary structure, disulfide bonds were not found between cysteine pairs: D. adjacent in the sequence [2]. In the intervening years it has bec ome apparent that all these forbidden regions are indeed occupied by disulfide-bonded cysteines, albeit rather strained ones. It has been observed that sources of strain in a protein structure, such as residues in forbidden regions of the Ramachandran plot and cis-peptide bonds, are found in functionally important regions of the protein and warrant further investigation [3-5]. Like the Ramachandran plot the earlier studies by Richardson [1] and Thomton [2] have identified a fundamental truth in protein stereo chem i stry: forbidden disulfides adopt strained conformations, but there is likely a functional reason for this. Emerging evidence supports a role for forbidden disulfides in redoxregulation of proteins.
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