1bkt

From Proteopedia

(Difference between revisions)

Revision as of 10:40, 19 May 2021

BMKTX TOXIN FROM SCORPION BUTHUS MARTENSII KARSCH, NMR, 25 STRUCTURES

Structural highlights

1bkt is a 1 chain structure with sequence from Buthus martensi. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[KAX36_MESMA] Blocks voltage-gated potassium channels. At 2 uM, blocks rat Kv1.1/KCNA1 and Kv1.3/KCNA3, has a strong effect on rat Kv1.2/KCNA2 and Kv1.6/KCNA6 as well as a moderate effect on Shaker IR.^[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

BmKTX is a toxin recently purified from the venom of Buthus Martensi, which belongs to the kaliotoxin family. We have determined its solution structure by use of conventional two-dimensional NMR techniques followed by distance-geometry and energy minimization. The calculated structure is composed of a short alpha-helix (residues 14 to 20) connected by a tight turn to a two-stranded antiparallel beta-sheet (sequences 25-27 and 32-34). The beta-turn connecting these strands belongs to type I. The N-terminal segment (sequence 1 to 8) runs parallel to the beta-sheet although it cannot be considered as a third strand. Comparison of the conformation of BmKTX and toxins of the kaliotoxin family clearly demonstrates that they are highly related. Therefore, analysis of the residues belonging to the interacting surface of those toxins allows us to propose a functional map of BmKTX slightly different from the one of KTX and AgTX2, which may explain the variations in affinities of these toxins towards the Kv1.3 channels.

Solution structure of BmKTX, a K+ blocker toxin from the Chinese scorpion Buthus Martensi.,Renisio JG, Romi-Lebrun R, Blanc E, Bornet O, Nakajima T, Darbon H Proteins. 2000 Jan 1;38(1):70-8. PMID:10651040^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Romi-Lebrun R, Lebrun B, Martin-Eauclaire MF, Ishiguro M, Escoubas P, Wu FQ, Hisada M, Pongs O, Nakajima T. Purification, characterization, and synthesis of three novel toxins from the Chinese scorpion Buthus martensi, which act on K+ channels. Biochemistry. 1997 Nov 4;36(44):13473-82. PMID:9354615 doi:http://dx.doi.org/10.1021/bi971044w
↑ Gao B, Peigneur S, Tytgat J, Zhu S. A potent potassium channel blocker from Mesobuthus eupeus scorpion venom. Biochimie. 2010 Dec;92(12):1847-53. doi: 10.1016/j.biochi.2010.08.003. Epub 2010 , Aug 14. PMID:20713119 doi:http://dx.doi.org/10.1016/j.biochi.2010.08.003
↑ Renisio JG, Romi-Lebrun R, Blanc E, Bornet O, Nakajima T, Darbon H. Solution structure of BmKTX, a K+ blocker toxin from the Chinese scorpion Buthus Martensi. Proteins. 2000 Jan 1;38(1):70-8. PMID:10651040

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1bkt"

@@ Line 3: / Line 3: @@
 <StructureSection load='1bkt' size='340' side='right'caption='[[1bkt]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1bkt]] 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=1BKT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BKT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1bkt]] 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=1BKT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BKT FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</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=1bkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bkt OCA], [http://pdbe.org/1bkt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bkt RCSB], [http://www.ebi.ac.uk/pdbsum/1bkt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bkt 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=1bkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bkt OCA], [https://pdbe.org/1bkt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bkt RCSB], [https://www.ebi.ac.uk/pdbsum/1bkt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bkt ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/KAX36_MESMA KAX36_MESMA]] Blocks voltage-gated potassium channels. At 2 uM, blocks rat Kv1.1/KCNA1 and Kv1.3/KCNA3, has a strong effect on rat Kv1.2/KCNA2 and Kv1.6/KCNA6 as well as a moderate effect on Shaker IR.<ref>PMID:9354615</ref> <ref>PMID:20713119</ref>
+[[https://www.uniprot.org/uniprot/KAX36_MESMA KAX36_MESMA]] Blocks voltage-gated potassium channels. At 2 uM, blocks rat Kv1.1/KCNA1 and Kv1.3/KCNA3, has a strong effect on rat Kv1.2/KCNA2 and Kv1.6/KCNA6 as well as a moderate effect on Shaker IR.<ref>PMID:9354615</ref> <ref>PMID:20713119</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 30: @@
 ==See Also==
-*[[Potassium channel toxin|Potassium channel toxin]]
+*[[Potassium channel toxin 3D structures|Potassium channel toxin 3D structures]]
 == References ==
 <references/>

1bkt

From Proteopedia

Revision as of 10:40, 19 May 2021

BMKTX TOXIN FROM SCORPION BUTHUS MARTENSII KARSCH, NMR, 25 STRUCTURES

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox