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2KGH

Solution structure of Brachyperma ruhnaui toxin 2

Summary for 2KGH
Entry DOI10.2210/pdb2kgh/pdb
DescriptorVenom peptide 2 (1 entity in total)
Functional Keywordsinsecticidal peptides, disulfide bond, neurotoxin, secreted, toxin
Biological sourceBrachypelma ruhnaui (Mexican golden redrump tarantula)
Cellular locationSecreted: P85504
Total number of polymer chains1
Total formula weight4457.55
Authors
Corzo, G.,Bernard, C.,Clement, H.,Bosmans, F.,Tygat, J.,Possani, L.D.,Darbon, H.,Alagon, A. (deposition date: 2009-03-12, release date: 2009-12-15, Last modification date: 2022-03-16)
Primary citationCorzo, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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