<unk>  is part of the Cystein-Rich Secretory Protein (CRISP) family. CRISPs comprise a particular group of snake venom proteins distributed among the venom of several families of snakes, such as elapids, colubrids and vipers. The protein exists of 240 amino acids, coded by an mRNA of 1336 base pairs. Structurally, it is composed of three distinct regions: an N-terminal protein domain, a hinge region and a C-terminal cystein-rich domain. It has a molecular mass of 25 kDa.<unk>  shows great sequence homology with triflin (83.7%) and latisemin (61.5%), two other snake venom components of the CRISP family, which also target voltage-dependent calcium channels. In addition, it shows partial homology with helothermine (52.8%), a venom protein of the Mexican beaded lizard; this protein, however, targets other ion channels than<unk> .
Ablomin
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Selpercatinib
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Phosgene
Brigatinib
Dosulepin
Tucatinib