2022
DOI: 10.1016/j.toxicon.2022.09.012
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Conformations of disulfides are conserved in inhibitory cystine knot (ICK) motif polypeptides

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“…This peptide is characterized by the classical consensus sequence CIX 2–7 -CIIX 3–11 -CIIIX 0–7 -CIVX 1–17 -CVX 1–19 -CVI and characteristic CI-CIV, CII-CV, and CIII-CVI disulfide bonds (the cysteine residues are labeled I–VI in order from the N- to the C-terminus), where X represents amino acids of varying lengths [ 10 , 15 , 16 , 17 ]. Typically, ICK contains three disulfide bonds in a sequence, with two disulfides forming the loop and the third disulfide penetrating through the loop [ 18 ]. This structure possesses exceptional stability, rendering peptides with the ICK motif, particularly those with additional disulfide bonds, highly resistant to denaturation and proteolysis.…”
Section: Structurementioning
confidence: 99%
“…This peptide is characterized by the classical consensus sequence CIX 2–7 -CIIX 3–11 -CIIIX 0–7 -CIVX 1–17 -CVX 1–19 -CVI and characteristic CI-CIV, CII-CV, and CIII-CVI disulfide bonds (the cysteine residues are labeled I–VI in order from the N- to the C-terminus), where X represents amino acids of varying lengths [ 10 , 15 , 16 , 17 ]. Typically, ICK contains three disulfide bonds in a sequence, with two disulfides forming the loop and the third disulfide penetrating through the loop [ 18 ]. This structure possesses exceptional stability, rendering peptides with the ICK motif, particularly those with additional disulfide bonds, highly resistant to denaturation and proteolysis.…”
Section: Structurementioning
confidence: 99%