1q2k

From Proteopedia

(Difference between revisions)

Revision as of 09:37, 8 September 2021

Solution structure of BmBKTx1 a new potassium channel blocker from the Chinese Scorpion Buthus martensi Karsch

Structural highlights

1q2k is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[KA191_MESMA] Selective inhibitor of high conductance calcium-activated potassium channels KCa1.1/KCNMA1. May be insect specific.^[1] [PDB:3E8Y]

Publication Abstract from PubMed

BmBKTx1 is a 31-amino acid peptide identified from the venom of the Chinese scorpion Buthus martensi Karsch, blocking high-conductance calcium-activated potassium channels. Sequence homology analysis indicates that BmBKTx1 is a new subfamily of short-chain alpha-KTx toxins of the potassium channel, which we term alpha-KTx19. Synthetic BmBKTx1 was prepared by using solid-phase peptide synthesis. Two-dimensional NMR spectroscopy techniques were used to determine the solution structure of BmBKTx1. The results show that the BmBKTx1 forms a typical cysteine-stabilized alpha/beta scaffold adopted by most short-chain scorpion toxins. The structure of BmBKTx1 consists of a two-stranded antiparallel beta-sheet (residues 20-29) and an alpha-helix (residues 5-15). The three-dimensional structure of BmBKTx1 was also compared with those of two function-related scorpion toxins, charybdotoxin (ChTx) and BmTx1, and their structural and functional implications are discussed.

Solution structure of BmBKTx1, a new BKCa1 channel blocker from the Chinese scorpion Buthus martensi Karsch.,Cai Z, Xu C, Xu Y, Lu W, Chi CW, Shi Y, Wu J Biochemistry. 2004 Apr 6;43(13):3764-71. PMID:15049683^[2]

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

References

↑ Xu CQ, Brone B, Wicher D, Bozkurt O, Lu WY, Huys I, Han YH, Tytgat J, Van Kerkhove E, Chi CW. BmBKTx1, a novel Ca2+-activated K+ channel blocker purified from the Asian scorpion Buthus martensi Karsch. J Biol Chem. 2004 Aug 13;279(33):34562-9. Epub 2004 Jun 3. PMID:15178692 doi:http://dx.doi.org/10.1074/jbc.M312798200
↑ Cai Z, Xu C, Xu Y, Lu W, Chi CW, Shi Y, Wu J. Solution structure of BmBKTx1, a new BKCa1 channel blocker from the Chinese scorpion Buthus martensi Karsch. Biochemistry. 2004 Apr 6;43(13):3764-71. PMID:15049683 doi:http://dx.doi.org/10.1021/bi035412+

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1q2k"

@@ Line 3: / Line 3: @@
 <StructureSection load='1q2k' size='340' side='right'caption='[[1q2k]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1q2k]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q2K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Q2K FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1q2k]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q2K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q2K FirstGlance]. <br>
-</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=1q2k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q2k OCA], [http://pdbe.org/1q2k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q2k RCSB], [http://www.ebi.ac.uk/pdbsum/1q2k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1q2k ProSAT]</span></td></tr>
+</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=1q2k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q2k OCA], [https://pdbe.org/1q2k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q2k RCSB], [https://www.ebi.ac.uk/pdbsum/1q2k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q2k ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/KA191_MESMA KA191_MESMA]] Selective inhibitor of high conductance calcium-activated potassium channels KCa1.1/KCNMA1. May be insect specific.<ref>PMID:15178692</ref> [PDB:3E8Y]
+[[https://www.uniprot.org/uniprot/KA191_MESMA KA191_MESMA]] Selective inhibitor of high conductance calcium-activated potassium channels KCa1.1/KCNMA1. May be insect specific.<ref>PMID:15178692</ref> [PDB:3E8Y]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 19: / Line 19: @@
 ==See Also==
-*[[Potassium channel toxin|Potassium channel toxin]]
+*[[Potassium channel toxin 3D structures|Potassium channel toxin 3D structures]]
 == References ==
 <references/>

1q2k

From Proteopedia

Revision as of 09:37, 8 September 2021

Solution structure of BmBKTx1 a new potassium channel blocker from the Chinese Scorpion Buthus martensi Karsch

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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