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1kba

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[[Image:1kba.png|left|200px]]
 
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==CRYSTAL STRUCTURE OF KAPPA-BUNGAROTOXIN AT 2.3-ANGSTROM RESOLUTION==
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The line below this paragraph, containing "STRUCTURE_1kba", creates the "Structure Box" on the page.
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<StructureSection load='1kba' size='340' side='right'caption='[[1kba]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<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>
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{{STRUCTURE_1kba| PDB=1kba | SCENE= }}
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kb/1kba_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1kba ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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., &amp; 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)
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===CRYSTAL STRUCTURE OF KAPPA-BUNGAROTOXIN AT 2.3-ANGSTROM RESOLUTION===
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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<ref>PMID:7947721</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_7947721}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1kba" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 7947721 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7947721}}
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==About this Structure==
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[[1kba]] is a 2 chain structure of [[Bungarotoxin]] with sequence from [http://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].
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==See Also==
==See Also==
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*[[Bungarotoxin]]
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*[[Bungarotoxin 3D structures|Bungarotoxin 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:7947721</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Bungarus multicinctus]]
[[Category: Bungarus multicinctus]]
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[[Category: Dewan, J C.]]
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[[Category: Large Structures]]
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[[Category: Grant, G A.]]
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[[Category: Dewan JC]]
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[[Category: Sacchettini, J C.]]
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[[Category: Grant GA]]
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[[Category: Toxin]]
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[[Category: Sacchettini JC]]

Current revision

CRYSTAL STRUCTURE OF KAPPA-BUNGAROTOXIN AT 2.3-ANGSTROM RESOLUTION

PDB ID 1kba

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