Solution structure of P01, a natural scorpion peptide structurally analogous to scorpion toxins specific for apamin-sensitive potassium channel

Blanc, Eric; Frémont, Valérie; Sizun, Philippe; Meunier, Sylvie; Rietschoten, J. Van; Thevand, A.; Bernassau, Jean‐Marie; Darbon, Hervé

doi:10.1002/(sici)1097-0134(199603)24:3<359::aid-prot9>3.0.co;2-b

Cited by 33 publications

(15 citation statements)

References 22 publications

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“…judaicus toxins share some sequence similarities with scorpion peptide P01 and leiuropeptide II, the solution structures of which have been determined by NMR spectroscopy (19,24). The backbone fold for all of these structurally identified peptides (listed in Fig.…”

Section: Purification Of B Judaicus Toxin Activators-[mentioning

confidence: 89%

“…Peptide P01 (19), the three-dimensional structure of which has been determined by NMR, is a natural peptide from the North African scorpion Androctonus mauretanicus mauretanicus. The primary structure of peptide P01 is quite similar to the B. judaicus toxins we purified, thus it was used as the structural model for building.…”

Section: Materials-[mentioning

confidence: 99%

“…B. judaicus toxins are highly homologous with scorpion peptide Lqhpep 2, from Leiurus quinquestriatus hebraeus (24), and PepII, from Buthus sindicus (25). They also share some similarity with peptide P01 from the scorpion A. mauretanicus mauretanicus, the three-dimensional structure of which has been determined by NMR (19). However, although the complete amino acid sequences of those three peptides have been determined, their biological function remains unknown.…”

Section: Purification Of B Judaicus Toxin Activators-[mentioning

confidence: 99%

“…3, the backbone model of BjTx-1 includes an ␣-helix connected by a tight turn to a ␤-sheet. The ␣-helix extends from residues Cys 3 to Gln 14 , with a Pro residue located at position 7, which may act as an ␣-helix breaker (19). The antiparallel ␤-sheet is composed of two strands.…”

Section: Purification Of B Judaicus Toxin Activators-[mentioning

confidence: 99%

“…The primary structures of both toxins are ordered as -Cys 1 -Cys 2 -Xaa-Xaa-Xaa-Cys 3 -Cys 4 -Cys 5 Xaa-Cys 6 -, a well known cysteine motif common to most scorpion toxins, including all the peptides we previously mentioned, and also charybdotoxin (26), iberiotoxin (27), margatoxin (28), and kaliotoxin (28). The ␣-helix and ␤-sheet are connected by three disulfide bridges, with the pattern Cys 1 -S-S-Cys 4 , Cys 2 -S-S-Cys 5 , and Cys 3 -S-S-Cys 6 (19).…”

Section: Purification Of B Judaicus Toxin Activators-[mentioning

confidence: 99%

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Activation of Skeletal Ryanodine Receptors by Two Novel Scorpion Toxins from Buthotus judaicus

Zhu

Zamudio

Olbinski

et al. 2004

Journal of Biological Chemistry

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Section: Purification Of B Judaicus Toxin Activators-[mentioning

confidence: 89%

Section: Materials-[mentioning

confidence: 99%

Section: Purification Of B Judaicus Toxin Activators-[mentioning

confidence: 99%

Section: Purification Of B Judaicus Toxin Activators-[mentioning

confidence: 99%

Section: Purification Of B Judaicus Toxin Activators-[mentioning

confidence: 99%

See 3 more Smart Citations

Activation of Skeletal Ryanodine Receptors by Two Novel Scorpion Toxins from Buthotus judaicus

Zhu

Zamudio

Olbinski

et al. 2004

Journal of Biological Chemistry

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Solution structure of maurotoxin, a scorpion toxin fromScorpio maurus, with high affinity for voltage-gated potassium channels

et al. 1997

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Maurotoxin (MTX), purified from the scorpionid Scorpio maurus is a potent ligand for potassium channels. It shows a broad specificity as being active on Kv1.1 (Kd = 37 nM), Kv1.2 (Kd = 0.8 nM), Kv1.3 (Kd = 150 nM) voltage-gated potassium channels, as well as on small-conductance calcium-activated potassium channels. It has a unique disulfide pairing among the scorpion toxins family. The solution structure of MTX has been determined by 2D-NMR techniques, which led to the full description of its 3D conformation: a bended helix from residues 6 to 16 connected by a loop to a two-stranded antiparallel beta sheet (residues 23 to 26 and 28 to 31). The interaction of MTX with the pore region of the Kv1.2 potassium channel has been modeled according to their charge anisotropy. The structure of MTX is similar to other short scorpion toxins despite its peculiar disulfide pairing. Its interaction with the Kv1.2 channel involves a dipole moment, which guides and orients the toxin onto the pore, toward the binding site, and which thus is responsible for the specificity.

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Solution structure of TsKapa, a charybdotoxin-like scorpion toxin fromTityus serrulatus with high affinity for apamin-sensitive Ca2+-activated K+ channels

et al. 1997

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TsKapa (TsK), purified from the Buthidae Tityus serrulatus is a very high potent ligand for small-conductance apamin-sensitive calcium-activated potassium channels (SK). It is able to efficiently compete with apamin for binding on this channel (K0.5 = 0.3 nM) [Legros, C. et al., FEBS Lett. 390:81-84, 1996]. The solution structure of TsK has been determined by 2D-NMR techniques, which led to the full description of its 3D conformation: a short alpha helix from residues 14 to 20 and a three-stranded antiparallel beta sheet (residues 2-3, 27-29, and 32-34). The interaction of TsK with the SK potassium channel has been modeled according to the charge anisotropy of the ligand. The resulting dipole moment orientates TsK so that it presents toward the receptor, a surface, mainly basic, encompassing residues K18 and K19 on one side and R9 and Y8 on the other. Despite its three-dimensional structure that is related with scorpion toxins active on voltage-gated potassium channels such as charybdotoxin, the pharmacological activity and specificity of TsK is related with shorter scorpion toxins (i.e., possessing an only two-stranded beta sheet) such as scyllatoxin (also named leiurotoxin I) or P05.

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Solution structure of P01, a natural scorpion peptide structurally analogous to scorpion toxins specific for apamin-sensitive potassium channel

Cited by 33 publications

References 22 publications

Activation of Skeletal Ryanodine Receptors by Two Novel Scorpion Toxins from Buthotus judaicus

Activation of Skeletal Ryanodine Receptors by Two Novel Scorpion Toxins from Buthotus judaicus

Solution structure of maurotoxin, a scorpion toxin fromScorpio maurus, with high affinity for voltage-gated potassium channels

Solution structure of TsKapa, a charybdotoxin-like scorpion toxin fromTityus serrulatus with high affinity for apamin-sensitive Ca2+-activated K+ channels

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