2008
DOI: 10.1107/s0907444908023512
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Structures of pseudechetoxin and pseudecin, two snake-venom cysteine-rich secretory proteins that target cyclic nucleotide-gated ion channels: implications for movement of the C-terminal cysteine-rich domain

Abstract: Cyclic nucleotide-gated (CNG) ion channels play pivotal roles in sensory transduction by retinal photoreceptors and olfactory neurons. The elapid snake toxins pseudechetoxin (PsTx) and pseudecin (Pdc) are the only known protein blockers of CNG channels. These toxins belong to a cysteinerich secretory protein (CRISP) family containing an N-terminal pathogenesis-related proteins of group 1 (PR-1) domain and a C-terminal cysteine-rich domain (CRD). PsTx and Pdc are highly homologous proteins, but their blocking a… Show more

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Cited by 63 publications
(49 citation statements)
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“…In this protein, the surface formed by the C-terminal-most region of the PR domain and a surface formed by the hinge domain face one another to provide a deep cleft that could be a site of protein docking. Indeed, binding of Zn 2+ by this protein results in a marked shift in the positions of these two surfaces, and the authors have postulated that this may regulate the interaction of this protein with the channel (Suzuki et al 2008 ). Similar tantalizing results come from our studies of peptides representing sequences within allurin that mimic this region of the PR and Hinge domains.…”
Section: The Future Of Crisp Protein Relationships In Reproductionsupporting
confidence: 69%
See 1 more Smart Citation
“…In this protein, the surface formed by the C-terminal-most region of the PR domain and a surface formed by the hinge domain face one another to provide a deep cleft that could be a site of protein docking. Indeed, binding of Zn 2+ by this protein results in a marked shift in the positions of these two surfaces, and the authors have postulated that this may regulate the interaction of this protein with the channel (Suzuki et al 2008 ). Similar tantalizing results come from our studies of peptides representing sequences within allurin that mimic this region of the PR and Hinge domains.…”
Section: The Future Of Crisp Protein Relationships In Reproductionsupporting
confidence: 69%
“…One possibility is that rather than acting independently, these two domains might both contribute surfaces that together allow new protein-protein interactions. An interesting piece of data that hints at this comes from the X-ray crystal structure of pseudecin, one of the Crisp protein snake toxins from the viper Pseudecis porphyriacus that inhibits cyclic nucleotide gated channels (Suzuki et al 2008 ). In this protein, the surface formed by the C-terminal-most region of the PR domain and a surface formed by the hinge domain face one another to provide a deep cleft that could be a site of protein docking.…”
Section: The Future Of Crisp Protein Relationships In Reproductionmentioning
confidence: 99%
“…Firstly, we formulated the hypothesis that the tandem histidine motif in Group 1 ASPs may be able to serve as a general metal binding site (Osman et al, 2012). Recent crystal structures have revealed that Group 1 ASPs bind zinc ions in this site; these include natrin (Wang et al,(37872)(37873)(37874)(37875)(37876)(37877)(37878)(37879)(37880)(37881)(37882)(37883), pseudecin (Suzuki et al, 2008) and GLIPR1 (Asojo et al, 2011). Secondly, we previously proposed that the shape and extent of the equatorial groove of Group 1 ASPs allows the binding of extended structures, such as peptides or glycans (Osman et al, 2012).…”
Section: Introductionmentioning
confidence: 99%
“…[20][21][22][23][24][25] Of note, it has been shown that the ability of the CRISP domain to regulate ion channel gating, for the King Brown snake CRISP pseudechetoxin, is enhanced by the presence of the CAP domain. 26 Specifically full-length pseudechetoxin at 100 nmol l 21 inhibited the cyclic nucleotide-gated ion channel A2, 30 times more potently than the ICR region of pseudechetoxin at 12 mmol l 21 .…”
Section: Crisp Structurementioning
confidence: 99%