Cysteine-rich secretory protein

Crisp domain (CRD)
The two domains of a Cysteine-rich secretory protein (CRISP).[1] CAP-like PR-1 domain in white. ShK-like CRD in red. Disulphides in yellow. Glycan chains not shown. (PDB: 1WVR​)
Identifiers
SymbolCrisp
PfamPF08562
Pfam clanCL0213
InterProIPR013871
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Cysteine-rich secretory proteins, often abbreviated as CRISPs, are a group of glycoproteins.[2] 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.[1] They are substantially implicated in the functioning of the mammalian reproductive system.[3] CRISPs are also found in a variety of snake venoms where they inhibit both smooth muscle contraction and cyclic nucleotide-gated ion channels.[4]

  1. ^ a b Guo M, Teng M, Niu L, Liu Q, Huang Q, Hao Q (April 2005). "Crystal structure of the cysteine-rich secretory protein stecrisp reveals that the cysteine-rich domain has a K+ channel inhibitor-like fold". The Journal of Biological Chemistry. 280 (13): 12405–12. doi:10.1074/jbc.M413566200. PMID 15596436.
  2. ^ Cite error: The named reference dictionary was invoked but never defined (see the help page).
  3. ^ Cite error: The named reference 25-Oct-2010 review was invoked but never defined (see the help page).
  4. ^ Cite error: The named reference Toxicon was invoked but never defined (see the help page).