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| <StructureSection load='2ybr' size='340' side='right'caption='[[2ybr]], [[Resolution|resolution]] 2.55Å' scene=''> | | <StructureSection load='2ybr' size='340' side='right'caption='[[2ybr]], [[Resolution|resolution]] 2.55Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[2ybr]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Cenno Cenno] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YBR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2YBR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ybr]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Centruroides_noxius Centruroides noxius] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YBR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YBR FirstGlance]. <br> |
- | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cn2|1cn2]], [[2yc1|2yc1]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55Å</td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2ybr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ybr OCA], [http://pdbe.org/2ybr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ybr RCSB], [http://www.ebi.ac.uk/pdbsum/2ybr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ybr ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ybr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ybr OCA], [https://pdbe.org/2ybr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ybr RCSB], [https://www.ebi.ac.uk/pdbsum/2ybr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ybr ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/SCX2_CENNO SCX2_CENNO]] Mammal beta-toxins bind voltage-independently at site-4 of sodium channels and shift the activation voltage to more negative potentials. This toxin is active against mammals. | + | [https://www.uniprot.org/uniprot/SCX2_CENNO SCX2_CENNO] Mammal beta-toxins bind voltage-independently at site-4 of sodium channels and shift the activation voltage to more negative potentials. This toxin is active against mammals. |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Cenno]] | + | [[Category: Centruroides noxius]] |
- | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Becerril, B]] | + | [[Category: Becerril B]] |
- | [[Category: Canul-Tec, J C]] | + | [[Category: Canul-Tec JC]] |
- | [[Category: Possani, L D]] | + | [[Category: Possani LD]] |
- | [[Category: Riano-Umbarila, L]] | + | [[Category: Riano-Umbarila L]] |
- | [[Category: Rudino-Pinera, E]] | + | [[Category: Rudino-Pinera E]] |
- | [[Category: Torres-Larios, A]] | + | [[Category: Torres-Larios A]] |
- | [[Category: Immune system-toxin complex]]
| + | |
- | [[Category: Scorpion toxin]]
| + | |
| Structural highlights
Function
SCX2_CENNO Mammal beta-toxins bind voltage-independently at site-4 of sodium channels and shift the activation voltage to more negative potentials. This toxin is active against mammals.
Publication Abstract from PubMed
It has previously been reported that several single-chain antibody fragments of human origin (scFv) neutralize the effects of two different scorpion venoms through interactions with the primary toxins of Centruroides noxius Hoffmann (Cn2) and Centruroides suffusus suffusus (Css2). Here we present the crystal structure of the complex formed between one scFv (9004G) and the Cn2 toxin, determined in two crystal forms at 2.5 and 1.9 A resolution. A 15-residue span of the toxin is recognized by the antibody through a cleft formed by residues from five of the complementarity-determining regions of the scFv. Analysis of the interface of the complex reveals three features. First, the epitope of toxin Cn2 overlaps with essential residues for the binding of beta-toxins to its Na(+) channel receptor site. Second, the putative recognition of Css2 involves mainly residues that are present in both Cn2 and Css2 toxins. Finally, the effect on the increase of affinity of previously reported key residues during the maturation process of different scFvs can be inferred from the structure. Taken together, these results provide the structural basis that explain the mechanism of the 9004G neutralizing activity and give insight into the process of directed evolution that gave rise to this family of neutralizing scFvs.
Structural Basis of Neutralization of the Major Toxic Component from the Scorpion Centruroides noxius Hoffmann by a Human-derived Single-chain Antibody Fragment.,Canul-Tec JC, Riano-Umbarila L, Rudino-Pinera E, Becerril B, Possani LD, Torres-Larios A J Biol Chem. 2011 Jun 10;286(23):20892-900. Epub 2011 Apr 13. PMID:21489992[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Canul-Tec JC, Riano-Umbarila L, Rudino-Pinera E, Becerril B, Possani LD, Torres-Larios A. Structural Basis of Neutralization of the Major Toxic Component from the Scorpion Centruroides noxius Hoffmann by a Human-derived Single-chain Antibody Fragment. J Biol Chem. 2011 Jun 10;286(23):20892-900. Epub 2011 Apr 13. PMID:21489992 doi:10.1074/jbc.M111.238410
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