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Dr Volker Herzig
Therapeutic applications of spider-venom peptides. In Glenn F. King Ed. Fry, B.
Roy , Gutierrez, J. Research methods. In Venomous reptiles and their toxins: evolution, pathophysiology and biodiscovery pp. Herzig, Volker and King, Glenn F. In Wolfgang Nentwig Ed. Herzig, V.
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Addendum: Spider toxins and their potential for insect control. In Lawrence I. Gilbert and Sarjeet S. Gill Ed. Lin King, John V. Cell , 6 : - Nixon, Samantha A. Veterinary Parasitology , 40 - Frontiers in Pharmacology , Herzig, Volker Arthropod assassins: crawling biochemists with diverse toxin pharmacopeias. Toxicon , 33 - Saez, Natalie J. Toxicon , - Herzig, Volker , King, Glenn F. Toxicon: X , Ma, Linlin , Chin, Yanni K. Biochemical Pharmacology , 60 - Toxins , 10 11 :.
Toxicon , 1 - 8. Biomedicines , 6 3 : Richards, Kay L. Proceedings of the National Academy of Sciences , Walker, Andrew A.
Nature Communications , 9 1 :. Pineda, Sandy S. Bioinformatics , 34 6 : - Sousa, Silmara R. PLoS One , 12 9 : e Hauke, Tobias J. Each toxin molecule is inserted between the principal and complementary faces of a subunit interface, where the tip of loop II occupies the agonist binding pocket underneath loop C, characterized by the disulfide bond between two adjacent cysteine residues at its tip. Positional reorganization of the two loops that border the binding pocket, i. In turn, residues on the loop II edge lay proximal to the complementary loop F, where they provide more minor contribution to complex cohesion.
Despite the use of another long neurotoxin and an engineered receptor, and apart from the tip of the toxin loop II being ca. Such differences may be due to the absence of a complementary subunit, which in pentameric complexes provides interactions that stabilize the toxin. All these complexes encompass an interfacial surface area between the bound 3FT and the subunit interface of ca.
These structural interpretations are fairly consistent with those raised from the mutagenesis data, including the nature of the pharmacophores involved into complex cohesion Fig.
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Here again, loop III does not contribute to the complex interface. Compared with structures of unbound Fas2 and AChE, the main rearrangements observed are associated with constraints in the inherent flexibility of the Fas2 loops and several AChE surface loops. These data suggested that MT7 binding requires a receptor dimer and primarily involves loop II of the toxin and the extracellular loop e2 of the receptor. In all these complexes, positively charged residues at the tip of the toxin loop II play a central role in the interaction, whereas on the target side, residues forming an aromatic pocket or surface are always implicated.
Mourier and coll. In turn, Ricciardi and coll.
Insect pharmacology : channels, receptors, toxins and enzymes in SearchWorks catalog
Several of these 3FPs have become useful tools for studying the function and the structure of their molecular targets. K and D. The authors declare no conflicts of interest.
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Volume , Issue S2. The full text of this article hosted at iucr. If you do not receive an email within 10 minutes, your email address may not be registered, and you may need to create a new Wiley Online Library account. If the address matches an existing account you will receive an email with instructions to retrieve your username. Journal of Neurochemistry Volume , Issue S2. Review Free Access. Denis Servent Corresponding Author E-mail address: denis. Tools Request permission Export citation Add to favorites Track citation.
Share Give access Share full text access. Share full text access. Please review our Terms and Conditions of Use and check box below to share full-text version of article. Figure 1 Open in figure viewer PowerPoint. The 3FP scaffold.