Cysteine-rich secretory protein
| Crisp domain (CRD) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Crisp | ||||||||
| Pfam | PF08562 | ||||||||
| Pfam clan | CL0213 | ||||||||
| InterPro | IPR013871 | ||||||||
| |||||||||
Cysteine-rich secretory proteins, often abbreviated as CRISPs, are a group of
cyclic nucleotide-gated ion channels.[4]
Structure
CRISPs contain two
CAP-like 'Pathogenesis-related 1' domain (PR-1), followed by the smaller ShK-like 'Cysteine-Rich Domain' (CRD).[1]
CRISPs are
disulfide bonds, particularly in the hinge region and CRD.[1]
Mammalian reproduction
CRISPs are found in the
During
contraceptives are being actively investigated.[3]
Snake venom
Ophiophagus hannah) for which the CRISP ophanin
is namedCRISPs are found in the
cyclic nucleotide-gated ion channels. One of the N. haje CRISPs was the first example of an acidic CRISP in reptilian venom. The selective ion channel activity of snake CRISPs, coupled with the variety of CRISPs available as the pool of venom proteins appears highly variable between (at least) cobra species, provide a valuable tool for probing the mechanisms of ion channel activity.[9]
References
- ^ PMID 15596436.
- ^ ISBN 0-19-852917-1. Retrieved October 27, 2010.
- ^ PMID 20972450.
- ^ PMID 15302528.
- ISBN 0-19-852917-1. Retrieved October 28, 2010.
- ^ PMID 12047379.
- ^ PMID 12646276.
- PMID 15953617.
- PMID 15670767.