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| | <StructureSection load='1kba' size='340' side='right'caption='[[1kba]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='1kba' size='340' side='right'caption='[[1kba]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1kba]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bunmu Bunmu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KBA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KBA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1kba]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KBA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KBA FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1nbt|1nbt]]</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]] 2.3Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kba OCA], [http://pdbe.org/1kba PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kba RCSB], [http://www.ebi.ac.uk/pdbsum/1kba PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kba 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=1kba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kba OCA], [https://pdbe.org/1kba PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kba RCSB], [https://www.ebi.ac.uk/pdbsum/1kba PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kba ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NXL1_BUNMU NXL1_BUNMU]] Neurotoxin. Binds and inhibits nicotinic acetylcholine receptors. Compared to alpha-neurotoxins, kappa-neurotoxins bind more strongly to neuronal receptors, and less strongly to muscle receptors.<ref>PMID:3986193</ref> | + | [https://www.uniprot.org/uniprot/3LKB_BUNMU 3LKB_BUNMU] Postsynaptic neurotoxin that binds and inhibits neuronal nicotinic acetylcholine receptors (nAChR) with high affinity (IC(50)<100 nM). Is a selective, and slowly reversible antagonist of alpha-3/CHRNA3-containing and some alpha-4/CHRNA4-containing AChRs.<ref>PMID:3986193</ref> <ref>PMID:9027980</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kb/1kba_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kb/1kba_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bunmu]] | + | [[Category: Bungarus multicinctus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dewan, J C]] | + | [[Category: Dewan JC]] |
| - | [[Category: Grant, G A]] | + | [[Category: Grant GA]] |
| - | [[Category: Sacchettini, J C]] | + | [[Category: Sacchettini JC]] |
| - | [[Category: Toxin]]
| + | |
| Structural highlights
Function
3LKB_BUNMU Postsynaptic neurotoxin that binds and inhibits neuronal nicotinic acetylcholine receptors (nAChR) with high affinity (IC(50)<100 nM). Is a selective, and slowly reversible antagonist of alpha-3/CHRNA3-containing and some alpha-4/CHRNA4-containing AChRs.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
kappa-Neurotoxins display a very low affinity for neuromuscular receptors, but bind tightly to, and inhibit, nicotinic acetylcholine receptors in neuronal tissue such as the chick ciliary ganglia. In contrast, alpha-neurotoxins bind with high affinity and inhibit nicotinic acetylcholine receptors at the neuromuscular junction. The origin of this difference in specificity has been a long-studied question in the field. Here we report the first crystal structure of a kappa-neurotoxin, kappa-bungarotoxin. Unlike the NMR structure previously reported [Sutcliffe, M. J., Dobson, C. M., & Oswald, R. E. (1992) Biochemistry 31, 2962-2970], the present crystal structure more accurately defines the polypeptide fold and the nature of the interaction between subunits in the active dimer, which is a unique feature of the kappa-neurotoxins. The structure has been refined to R = 19.6% with X-ray diffraction data extending to a resolution of 2.3 A. There are two independent protein molecules (66 amino acid residues each) in the asymmetric unit that are arranged as a dimer with the two subunits related by a rotation of 178.6 degrees. Each subunit consists of three main-chain loops. Three of the five beta-strands of each subunit form an antiparallel beta-sheet which becomes an extended six-stranded antiparallel beta-sheet, by virtue of the approximate 2-fold symmetry of the dimer. The interactions at the dimer interface consist of six main-chain-main-chain hydrogen bonds, as well as three other hydrogen-bonding interactions involving side chains.(ABSTRACT TRUNCATED AT 250 WORDS)
Crystal structure of kappa-bungarotoxin at 2.3-A resolution.,Dewan JC, Grant GA, Sacchettini JC Biochemistry. 1994 Nov 8;33(44):13147-54. PMID:7947721[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Grant GA, Chiappinelli VA. kappa-Bungarotoxin: complete amino acid sequence of a neuronal nicotinic receptor probe. Biochemistry. 1985 Mar 12;24(6):1532-7. PMID:3986193
- ↑ Chiappinelli VA, Weaver WR, McLane KE, Conti-Fine BM, Fiordalisi JJ, Grant GA. Binding of native kappa-neurotoxins and site-directed mutants to nicotinic acetylcholine receptors. Toxicon. 1996 Nov-Dec;34(11-12):1243-56. PMID:9027980 doi:10.1016/s0041-0101(96)00110-9
- ↑ Dewan JC, Grant GA, Sacchettini JC. Crystal structure of kappa-bungarotoxin at 2.3-A resolution. Biochemistry. 1994 Nov 8;33(44):13147-54. PMID:7947721
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