1big: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
 ==SCORPION TOXIN BMTX1 FROM BUTHUS MARTENSII KARSCH, NMR, 25 STRUCTURES==
-<StructureSection load='1big' size='340' side='right'caption='[[1big]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>
+<StructureSection load='1big' size='340' side='right'caption='[[1big]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1big]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buthus_martensi Buthus martensi]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BIG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BIG FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1big]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mesobuthus_martensii Mesobuthus martensii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BIG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BIG FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></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=1big FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1big OCA], [https://pdbe.org/1big PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1big RCSB], [https://www.ebi.ac.uk/pdbsum/1big PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1big ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/KAX15_MESMA KAX15_MESMA]] Potent blocker of both large-conductance calcium-activated potassium channels (BKCa channels) and voltage-gated potassium channels (Kv1.3/KCNA3).<ref>PMID:9354615</ref>
+[https://www.uniprot.org/uniprot/KAX15_MESMA KAX15_MESMA] Potent blocker of both large-conductance calcium-activated potassium channels (BKCa channels) and voltage-gated potassium channels (Kv1.3/KCNA3).<ref>PMID:9354615</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 19: / Line 20: @@
 </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=1big ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The solution structure of BmTX2 purified from the venom of the Chinese Buthid Buthus martensi has been determined by 2D NMR spectroscopy techniques which led to the description of its 3D conformation. The structure consists of a triple-stranded beta-sheet connected to a helical structure. This helix encompasses 10 residues, from 11 to 20, begins with a turn of 310 helix, and ends with an alpha helix. The three strands of beta sheet comprise residues 2-6, with a bulge covering residues 4 and 5, 26-29, and 32-35, with a type I' beta turn centered on residues 30-31. We also characterized the solution structure of BmTX1. The two toxins which are potent blockers of both large-conductance calcium-activated potassium channels (BKCa channels) and voltage-gated potassium channels (Kv1. 3) are highly superimposable and possess the same structural characteristics. Analysis of these structures allows us to hypothesize that, besides the main surface of interaction described by the functional map of charybdotoxin, one can expect that the binding of scorpion toxins on BKCa channels may involve residues on the edge of this surface.
-Solution structure of two new toxins from the venom of the Chinese scorpion Buthus martensi Karsch blockers of potassium channels.,Blanc E, Romi-Lebrun R, Bornet O, Nakajima T, Darbon H Biochemistry. 1998 Sep 8;37(36):12412-8. PMID:9730813<ref>PMID:9730813</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1big" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 35: / Line 27: @@
 __TOC__
 </StructureSection>
-[[Category: Buthus martensi]]
 [[Category: Large Structures]]
-[[Category: Blanc, E]]
+[[Category: Mesobuthus martensii]]
-[[Category: Bornet, O]]
+[[Category: Blanc E]]
-[[Category: Darbon, H]]
+[[Category: Bornet O]]
-[[Category: Nakajima, T]]
+[[Category: Darbon H]]
-[[Category: Romi-Lebrun, R]]
+[[Category: Nakajima T]]
-[[Category: Buthus martensii]]
+[[Category: Romi-Lebrun R]]
-[[Category: Large conductance potassium channel]]
-[[Category: Neurotoxin]]
-[[Category: Scorpion]]
-[[Category: Toxin]]
-[[Category: Voltage gated potassium channel]]