1big: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==SCORPION TOXIN BMTX1 FROM BUTHUS MARTENSII KARSCH, NMR, 25 STRUCTURES== | ==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]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''> | ||
| Line 4: | Line 5: | ||
<table><tr><td colspan='2'>[[1big]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BIG FirstGlance]. <br> | <table><tr><td colspan='2'>[[1big]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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='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> | ||
<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=1big FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1big OCA], [http://pdbe.org/1big PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1big RCSB], [http://www.ebi.ac.uk/pdbsum/1big PDBsum]</span></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=1big FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1big OCA], [http://pdbe.org/1big PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1big RCSB], [http://www.ebi.ac.uk/pdbsum/1big PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1big ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| Line 29: | Line 30: | ||
==See Also== | ==See Also== | ||
*[[ | *[[User:Eric Martz/Entertaining PDB codes|User:Eric Martz/Entertaining PDB codes]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 14:03, 22 November 2017
SCORPION TOXIN BMTX1 FROM BUTHUS MARTENSII KARSCH, NMR, 25 STRUCTURESSCORPION TOXIN BMTX1 FROM BUTHUS MARTENSII KARSCH, NMR, 25 STRUCTURES
Structural highlights
Function[KAX15_MESMA] Potent blocker of both large-conductance calcium-activated potassium channels (BKCa channels) and voltage-gated potassium channels (Kv1.3/KCNA3).[1] 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 PubMedThe 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||