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Cysteine-rich secretory protein
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Cysteine-rich secretory protein : ウィキペディア英語版
Cysteine-rich secretory protein
Cysteine-rich secretory proteins, often abbreviated as CRISPs, are a group of glycoproteins.〔 They are a subgroup of the CRISP, antigen 5 and Pr-1 (CAP) protein superfamily and are substantially implicated in the functioning of the mammalian reproductive system.〔 CRISPs are also found in a variety of snake venoms where they inhibit both smooth muscle contraction and cyclic nucleotide-gated ion channels.〔
== Structure ==

Glycoproteins are conjugated proteins in which the non-protein group is a carbohydrate glycan – typically an oligosaccharide or small polysaccharide, but occasionally a monosaccharide. The glycan is covalently bound to a side chain of the polypeptide, rather than to the C- or N-terminus of the protein in a process called glycosylation. CRISPs are glycoproteins in which the primary structure is rich in the amino acid cysteine. Cysteine residues are typically oxidised to cystine in proteins, as the formation of disulfide bonds plays an important role in protein folding and the stabilisation of tertiary structure – this is particularly important with proteins secreted to the extracellular medium such as CRISPs. However, CRISPs are atypical in that they often possess significant numbers of native (unoxidised) cysteine residues in addition to cystine residues involved in disulfide bonds. The
King Cobra venom ophanin,〔 for example, has 16 strictly conserved cysteines in addition to 8 disulfide bonds.

抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)
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