1ter

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(Difference between revisions)

Revision as of 09:26, 29 September 2021

SOLUTION STRUCTURE OF TERTIAPIN DETERMINED USING NUCLEAR MAGNETIC RESONANCE AND DISTANCE GEOMETRY

Structural highlights

1ter is a 1 chain structure with sequence from Apime. 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

[TERT_APIME] Presynaptic neurotoxin that blocks the inwardly rectifying Kir1.1/KCNJ1 and Kir3.1/3.4 (KCNJ3/KCNJ5) potassium channels with high affinity by binding to the M1-M2 linker region of these channels in a 1:1 stoichiometry. It may block the potassium channel pore by occluding its alpha helix into the channel vestibule. Tertiapin-Q also inhibits calcium-activated large conductance BK-type (KCNMA) potassium channels in a concentration-, and voltage-dependent manner, in addition to inhibiting Kir3.1/3.2 (KCNJ3/KCNJ6) heteromultimers potassium channels. It can prevent dose-dependently acetylcholine(ACh)-induced atrioventricular blocks in mammalian hearts, as KCNJ3/KCNJ5 channels (also named I(KACh), because these channels are activated by ACh) are found in mammalian myocytes. Interacts specifically with calmodulin in the presence of calcium.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7]

Publication Abstract from PubMed

The solution structure of tertiapin, a 21-residue bee venom peptide, has been characterized by circular dichroism (CD), two-dimensional nuclear magnetic resonance (NMR) spectroscopy, and distance geometry. A total of 21 lowest error structures were obtained from distance geometry calculations. Superimposition of these structures shows that the backbone of tertiapin is very well defined. One type-I reverse turn from residue 4 to 7 and an alpha-helix from residue 12 to 19 exist in the structure of tertiapin. The alpha-helical region is best defined from both conformational analysis and structural superimposition. The overall three-dimensional structure of tertiapin is highly compact resulting from side chain interactions. The structural information obtained from CD and NMR are compared for both tertiapin and apamin (ref. 3), another bee venom peptide. Tertiapin and apamin have some similar secondary structure, but display different tertiary structures.

Solution structure of tertiapin determined using nuclear magnetic resonance and distance geometry.,Xu X, Nelson JW Proteins. 1993 Oct;17(2):124-37. PMID:8265561^[8]

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

References

↑ Jin W, Lu Z. A novel high-affinity inhibitor for inward-rectifier K+ channels. Biochemistry. 1998 Sep 22;37(38):13291-9. PMID:9748337 doi:http://dx.doi.org/10.1021/bi981178p
↑ Miroshnikov AI, Boikov VA, Snezhkova LG, Severin SE, Shvets VI. [Interaction of tertiapin, a neurotoxin from bee venom, with calmodulin] Bioorg Khim. 1983 Jan;9(1):26-32. PMID:6091685
↑ Jin W, Klem AM, Lewis JH, Lu Z. Mechanisms of inward-rectifier K+ channel inhibition by tertiapin-Q. Biochemistry. 1999 Oct 26;38(43):14294-301. PMID:10572004
↑ Drici MD, Diochot S, Terrenoire C, Romey G, Lazdunski M. The bee venom peptide tertiapin underlines the role of I(KACh) in acetylcholine-induced atrioventricular blocks. Br J Pharmacol. 2000 Oct;131(3):569-77. PMID:11015309 doi:http://dx.doi.org/10.1038/sj.bjp.0703611
↑ Kitamura H, Yokoyama M, Akita H, Matsushita K, Kurachi Y, Yamada M. Tertiapin potently and selectively blocks muscarinic K(+) channels in rabbit cardiac myocytes. J Pharmacol Exp Ther. 2000 Apr;293(1):196-205. PMID:10734170
↑ Kanjhan R, Coulson EJ, Adams DJ, Bellingham MC. Tertiapin-Q blocks recombinant and native large conductance K+ channels in a use-dependent manner. J Pharmacol Exp Ther. 2005 Sep;314(3):1353-61. Epub 2005 Jun 9. PMID:15947038 doi:http://dx.doi.org/jpet.105.085928
↑ Hashimoto N, Yamashita T, Tsuruzoe N. Tertiapin, a selective IKACh blocker, terminates atrial fibrillation with selective atrial effective refractory period prolongation. Pharmacol Res. 2006 Aug;54(2):136-41. Epub 2006 Apr 1. PMID:16725344 doi:http://dx.doi.org/S1043-6618(06)00059-4
↑ Xu X, Nelson JW. Solution structure of tertiapin determined using nuclear magnetic resonance and distance geometry. Proteins. 1993 Oct;17(2):124-37. PMID:8265561 doi:http://dx.doi.org/10.1002/prot.340170203

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

Categories: Apime | Large Structures | Nelson, J W | Xu, X | Toxin

@@ Line 3: / Line 3: @@
 <StructureSection load='1ter' size='340' side='right'caption='[[1ter]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ter]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Apime Apime]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TER OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TER FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ter]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Apime Apime]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TER OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TER 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=1ter FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ter OCA], [http://pdbe.org/1ter PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ter RCSB], [http://www.ebi.ac.uk/pdbsum/1ter PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ter 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=1ter FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ter OCA], [https://pdbe.org/1ter PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ter RCSB], [https://www.ebi.ac.uk/pdbsum/1ter PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ter ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/TERT_APIME TERT_APIME]] Presynaptic neurotoxin that blocks the inwardly rectifying Kir1.1/KCNJ1 and Kir3.1/3.4 (KCNJ3/KCNJ5) potassium channels with high affinity by binding to the M1-M2 linker region of these channels in a 1:1 stoichiometry. It may block the potassium channel pore by occluding its alpha helix into the channel vestibule. Tertiapin-Q also inhibits calcium-activated large conductance BK-type (KCNMA) potassium channels in a concentration-, and voltage-dependent manner, in addition to inhibiting Kir3.1/3.2 (KCNJ3/KCNJ6) heteromultimers potassium channels. It can prevent dose-dependently acetylcholine(ACh)-induced atrioventricular blocks in mammalian hearts, as KCNJ3/KCNJ5 channels (also named I(KACh), because these channels are activated by ACh) are found in mammalian myocytes. Interacts specifically with calmodulin in the presence of calcium.<ref>PMID:9748337</ref> <ref>PMID:6091685</ref> <ref>PMID:10572004</ref> <ref>PMID:11015309</ref> <ref>PMID:10734170</ref> <ref>PMID:15947038</ref> <ref>PMID:16725344</ref>
+[[https://www.uniprot.org/uniprot/TERT_APIME TERT_APIME]] Presynaptic neurotoxin that blocks the inwardly rectifying Kir1.1/KCNJ1 and Kir3.1/3.4 (KCNJ3/KCNJ5) potassium channels with high affinity by binding to the M1-M2 linker region of these channels in a 1:1 stoichiometry. It may block the potassium channel pore by occluding its alpha helix into the channel vestibule. Tertiapin-Q also inhibits calcium-activated large conductance BK-type (KCNMA) potassium channels in a concentration-, and voltage-dependent manner, in addition to inhibiting Kir3.1/3.2 (KCNJ3/KCNJ6) heteromultimers potassium channels. It can prevent dose-dependently acetylcholine(ACh)-induced atrioventricular blocks in mammalian hearts, as KCNJ3/KCNJ5 channels (also named I(KACh), because these channels are activated by ACh) are found in mammalian myocytes. Interacts specifically with calmodulin in the presence of calcium.<ref>PMID:9748337</ref> <ref>PMID:6091685</ref> <ref>PMID:10572004</ref> <ref>PMID:11015309</ref> <ref>PMID:10734170</ref> <ref>PMID:15947038</ref> <ref>PMID:16725344</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

1ter

From Proteopedia

Revision as of 09:26, 29 September 2021

SOLUTION STRUCTURE OF TERTIAPIN DETERMINED USING NUCLEAR MAGNETIC RESONANCE AND DISTANCE GEOMETRY

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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