Cysteine-rich secretory protein
protein family
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 also contain a domain related to the ShK toxins. They 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
CRISPs contain two domains joined by a hinge region. The larger domain is a CAP-like 'Pathogenesis-related 1' domain (PR-1), followed by the smaller ShK-like 'Cysteine-Rich Domain' (CRD).
CRISPs are glycoproteins, with a number of carbohydrate glycans covalently attached to amino acid side-chains on their surface via glycosylation. The primary structure is also rich in cysteine that form disulfide bonds, particularly in the hinge region and CRD.
Mammalian reproduction
CRISPs are found in the testes and epididymis of mammals, and are also involved in the process of fertilisation. In the spermatogenesis process (development of the spermatozoa in the testis), the CRISP2 protein is incorporated into the acrosome where it is believed to be involved in the adhesion of germ cells with Sertoli cells. CRISP2 also forms part of the sperm tail where it is thought to be involved in regulating flagellar beating.
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