1hvw
From Proteopedia
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[[Image:1hvw.gif|left|200px]] | [[Image:1hvw.gif|left|200px]] | ||
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| - | + | {{STRUCTURE_1hvw| PDB=1hvw | SCENE= }} | |
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'''HAIRPINLESS MUTANT OF OMEGA-ATRACOTOXIN-HV1A''' | '''HAIRPINLESS MUTANT OF OMEGA-ATRACOTOXIN-HV1A''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HVW is a [[Single protein]] structure | + | 1HVW is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HVW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Fletcher, J I.]] | [[Category: Fletcher, J I.]] | ||
[[Category: King, G F.]] | [[Category: King, G F.]] | ||
| - | [[Category: | + | [[Category: Beta-hairpin]] |
| - | [[Category: | + | [[Category: Cystine knot]] |
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Revision as of 16:17, 2 May 2008
HAIRPINLESS MUTANT OF OMEGA-ATRACOTOXIN-HV1A
Overview
omega-Atracotoxin-Hv1a is an insect-specific neurotoxin whose phylogenetic specificity derives from its ability to antagonize insect, but not vertebrate, voltage-gated calcium channels. In order to help understand its mechanism of action and to enhance its utility as a lead compound for insecticide development, we used a combination of protein engineering and site-directed mutagenesis to probe the toxin for key functional regions. First, we constructed a Hairpinless mutant in which the C-terminal beta-hairpin, which is highly conserved in this family of neurotoxins, was excised without affecting the fold of the residual disulfide-rich core of the toxin. The Hairpinless mutant was devoid of insecticidal activity, indicating the functional importance of the hairpin. We subsequently developed a highly efficient system for production of recombinant toxin and then probed the hairpin for key functional residues using alanine-scanning mutagenesis followed by a second round of mutagenesis based on initial "hits" from the alanine scan. This revealed that two spatially proximal residues, Asn(27) and Arg(35), form a contiguous molecular surface that is essential for toxin activity. We propose that this surface of the beta-hairpin is a key site for interaction of the toxin with insect calcium channels.
About this Structure
1HVW is a Single protein structure. Full crystallographic information is available from OCA.
Reference
Functional significance of the beta hairpin in the insecticidal neurotoxin omega-atracotoxin-Hv1a., Tedford HW, Fletcher JI, King GF, J Biol Chem. 2001 Jul 13;276(28):26568-76. Epub 2001 Apr 19. PMID:11313356 Page seeded by OCA on Fri May 2 19:17:00 2008
