2KGH

Solution structure of Brachyperma ruhnaui toxin 2

2KGH の概要

• エントリーDOI: 10.2210/pdb2kgh/pdb
• 分子名称: Venom peptide 2 (1 entity in total)
• 機能のキーワード: insecticidal peptides, disulfide bond, neurotoxin, secreted, toxin
• 由来する生物種: Brachypelma ruhnaui (Mexican golden redrump tarantula)
• 細胞内の位置: Secreted: P85504
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4457.55

構造登録者

Corzo, G.,Bernard, C.,Clement, H.,Bosmans, F.,Tygat, J.,Possani, L.D.,Darbon, H.,Alagon, A. (登録日: 2009-03-12, 公開日: 2009-12-15, 最終更新日: 2022-03-16)

主引用文献

Corzo, G.,Bernard, C.,Clement, H.,Villegas, E.,Bosmans, F.,Tytgat, J.,Possani, L.D.,Darbon, H.,Alagon, A.
Insecticidal peptides from the theraposid spider Brachypelma albiceps: an NMR-based model of Ba2.
Biochim.Biophys.Acta, 1794:1190-1196, 2009

PubMed Abstract: Soluble venom and purified fractions of the theraposid spider Brachypelma albiceps were screened for insecticidal peptides based on toxicity to crickets. Two insecticidal peptides, named Ba1 and Ba2, were obtained after the soluble venom was separated by high performance liquid chromatography and cation exchange chromatography. The two insecticidal peptides contain 39 amino acid residues and three disulfide bonds, and based on their amino acid sequence, they are highly identical to the insecticidal peptides from the theraposid spiders Aphonopelma sp. from the USA and Haplopelma huwenum from China indicating a relationship among these genera. Although Ba1 and Ba2 were not able to modify currents in insect and vertebrate cloned voltage-gated sodium ion channels, they have noteworthy insecticidal activities compared to classical arachnid insecticidal toxins indicating that they might target unknown receptors in insect species. The most abundant insecticidal peptide Ba2 was submitted to NMR spectroscopy to determine its 3-D structure; a remarkable characteristic of Ba2 is a cluster of basic residues, which might be important for receptor recognition.

PubMed: 19374957
DOI: 10.1016/j.bbapap.2009.04.004

実験手法

SOLUTION NMR