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A cystine knot is a protein structural motif containing three disulfide bridges (formed from pairs of cysteine residues). The sections of polypeptide that occur between two of them form a loop through which a third disulfide bond passes, forming a rotaxane substructure. It occurs in many proteins across many species and provides considerable structural stability.〔(http://www.cyclotide.com/knots.html )〕 There are three types of cystine knot, which differ in the topology of the disulfide bonds: * The Growth Factor Cystine Knot (GFCK) * Inhibitor Cystine Knot (ICK) common in spider and snail toxins * Cyclic Cystine Knot, or cyclotide The growth factor cystine knot (GFCK) was first observed in the structure of Nerve Growth Factor, solved by X-ray crystallography and published in 1991 by Tom Blundell in Nature.〔; 〕 All GFCK structures that have been determined are dimeric, but their dimerization modes in different classes are different. ==References== 抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)』 ■ウィキペディアで「Cystine knot」の詳細全文を読む スポンサード リンク
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