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==THE CRYSTAL STRUCTURE OF NEUROTOXIN-I FROM NAJA NAJA OXIANA AT 1.9 ANGSTROMS RESOLUTION== | ==THE CRYSTAL STRUCTURE OF NEUROTOXIN-I FROM NAJA NAJA OXIANA AT 1.9 ANGSTROMS RESOLUTION== | ||
<StructureSection load='1ntn' size='340' side='right' caption='[[1ntn]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1ntn' size='340' side='right'caption='[[1ntn]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ntn]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1ntn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Naja_oxiana Naja oxiana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NTN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NTN FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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=1ntn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ntn OCA], [https://pdbe.org/1ntn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ntn RCSB], [https://www.ebi.ac.uk/pdbsum/1ntn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ntn ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/3L21_NAJOX 3L21_NAJOX] Binds with high affinity to muscular (tested on Torpedo marmorata AChR, Kd=0.38 nM) and neuronal (tested on chimeric alpha-7/CHRNA7, Kd=12 nM) nicotinic acetylcholine receptor (nAChR) and inhibits acetylcholine from binding to the receptor, thereby impairing neuromuscular and neuronal transmission (PubMed:9305882). The toxin also shows a very weak inhibition of GABA(A) receptors composed of alpha-1-beta-3-gamma-2 (GABRA1-GABRB3-GABRG2) subunits (PubMed:26221036).<ref>PMID:26221036</ref> <ref>PMID:9305882</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nt/1ntn_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nt/1ntn_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <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> | ||
</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/ | </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=1ntn ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Betzel | [[Category: Naja oxiana]] | ||
[[Category: Mikhailov | [[Category: Betzel C]] | ||
[[Category: Nickitenko | [[Category: Mikhailov AM]] | ||
[[Category: Vainshtein | [[Category: Nickitenko AV]] | ||
[[Category: Wilson | [[Category: Vainshtein BK]] | ||
[[Category: Wilson K]] |
Latest revision as of 10:06, 30 October 2024
THE CRYSTAL STRUCTURE OF NEUROTOXIN-I FROM NAJA NAJA OXIANA AT 1.9 ANGSTROMS RESOLUTIONTHE CRYSTAL STRUCTURE OF NEUROTOXIN-I FROM NAJA NAJA OXIANA AT 1.9 ANGSTROMS RESOLUTION
Structural highlights
Function3L21_NAJOX Binds with high affinity to muscular (tested on Torpedo marmorata AChR, Kd=0.38 nM) and neuronal (tested on chimeric alpha-7/CHRNA7, Kd=12 nM) nicotinic acetylcholine receptor (nAChR) and inhibits acetylcholine from binding to the receptor, thereby impairing neuromuscular and neuronal transmission (PubMed:9305882). The toxin also shows a very weak inhibition of GABA(A) receptors composed of alpha-1-beta-3-gamma-2 (GABRA1-GABRB3-GABRG2) subunits (PubMed:26221036).[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 PubMedNeurotoxin-1 from Naja naja oxiana venom (NTX-1) has been crystallized by vapor diffusion in sitting drops. The crystals have cell dimensions of a = 25.2 A, b = 75.6 A, c = 35.9 A, and are in space group P2(1)2(1)2(1). Three-dimensional data to 1.9 A have been recorded by a Syntex P2(1) automatic diffractometer. The atomic structure of the toxin has been determined by molecular replacement using the alpha-cobratoxin (alpha-CTX) as the search model. The position of 534 non-hydrogen protein atoms have been determined. The model contains 65 water molecules. Refinement has led to an R-factor of 19.3% at 1.9 A resolution. The secondary and tertiary structures of NTX-1 have been analyzed and a comparison with structure of the alpha-CTX has been made. Three-dimensional structure of neurotoxin-1 from Naja naja oxiana venom at 1.9 A resolution.,Nickitenko AV, Michailov AM, Betzel C, Wilson KS FEBS Lett. 1993 Apr 5;320(2):111-7. PMID:8458425[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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