1qmw

From Proteopedia

(Difference between revisions)

Current revision

Solution structure of alpha-conotoxin SI

Structural highlights

1qmw is a 1 chain structure with sequence from Conus striatus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR, 36 models
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CA1_CONST Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them (PubMed:3196703). Is active on muscle nAChR (IC(50)=113 nM on adult subtype (alpha-1-beta-1-gamma-delta/CHRNA1-CHRNB1-CHRNG-CHRND) and IC(50)=142 nM on fetal subtype (alpha-1-beta-1-delta-epsilon/CHRNA1-CHRNB1-CHRND-CHRNE)) (PubMed:35357806, PubMed:9174364). On mice muscle receptors, its higher affinity site is the alpha/delta nAChR subunit interface (PubMed:9174364). On Torpedo receptors, it does not distinguish between alpha/delta and alpha/gamma acetylcholine-binding sites (PubMed:9174364). In vivo, causes paralysis followed by death when injected into goldfish (PubMed:3196703). In contrast, has no effect on mice, when similar doses are intraperitoneally or intracerebrally injected (PubMed:3196703).^[1] ^[2] ^[3]

Publication Abstract from PubMed

The nuclear magnetic resonance solution structure of alpha-conotoxin SI has been determined at pH 4.2. The 36 lowest energy structures show that alpha-conotoxin SI exists in a single major solution conformation and is stabilized by six hydrogen bonds. Comparisons are made between the SI solution structure and the solution and crystal structures of alpha-conotoxin GI. Surprisingly, a high degree of similarity between the backbone conformations of the GI crystal and the SI solution structures is seen in the region of lowest sequence homology, namely residues Gly-8 to Ser-12. This similarity is more surprising when considering that in SI a proline replaces the Arg-9 found in GI. The correspondence in conformation in this region provides the definitive evidence that it is the loss of the arginine basic charge at residue 9 which determines the differences in toxicity between GI and SI, rather than any changes in conformation induced by the cyclic proline residue.

Solution structure of alpha-conotoxin SI.,Benie AJ, Whitford D, Hargittai B, Barany G, Janes RW FEBS Lett. 2000 Jul 7;476(3):287-95. PMID:10913630^[4]

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

References

↑ Zafaralla GC, Ramilo C, Gray WR, Karlstrom R, Olivera BM, Cruz LJ. Phylogenetic specificity of cholinergic ligands: alpha-conotoxin SI. Biochemistry. 1988 Sep 6;27(18):7102-5. PMID:3196703 doi:10.1021/bi00418a065
↑ Wilhelm P, Luna-Ramirez K, Chin YK, Dekan Z, Abraham N, Tae HS, Chow CY, Eagles DA, King GF, Lewis RJ, Adams DJ, Alewood PF. Cysteine-Rich α-Conotoxin SII Displays Novel Interactions at the Muscle Nicotinic Acetylcholine Receptor. ACS Chem Neurosci. 2022 Apr 20;13(8):1245-1250. PMID:35357806 doi:10.1021/acschemneuro.1c00857
↑ Groebe DR, Gray WR, Abramson SN. Determinants involved in the affinity of alpha-conotoxins GI and SI for the muscle subtype of nicotinic acetylcholine receptors. Biochemistry. 1997 May 27;36(21):6469-74. PMID:9174364 doi:10.1021/bi970195w
↑ Benie AJ, Whitford D, Hargittai B, Barany G, Janes RW. Solution structure of alpha-conotoxin SI. FEBS Lett. 2000 Jul 7;476(3):287-95. PMID:10913630

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/1qmw"

@@ Line 1: / Line 1: @@
-==SOLUTION STRUCTURE OF ALPHA-CONOTOXIN SI==
-<StructureSection load='1qmw' size='340' side='right' caption='[[1qmw]], [[NMR_Ensembles_of_Models | 36 NMR models]]' scene=''>
+==Solution structure of alpha-conotoxin SI==
+<StructureSection load='1qmw' size='340' side='right'caption='[[1qmw]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1qmw]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QMW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QMW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1qmw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Conus_striatus Conus striatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QMW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QMW FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 36 models</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qmw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qmw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qmw RCSB], [http://www.ebi.ac.uk/pdbsum/1qmw PDBsum]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
-<table>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qmw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qmw OCA], [https://pdbe.org/1qmw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qmw RCSB], [https://www.ebi.ac.uk/pdbsum/1qmw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qmw ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CA1_CONST CA1_CONST] Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them (PubMed:3196703). Is active on muscle nAChR (IC(50)=113 nM on adult subtype (alpha-1-beta-1-gamma-delta/CHRNA1-CHRNB1-CHRNG-CHRND) and IC(50)=142 nM on fetal subtype (alpha-1-beta-1-delta-epsilon/CHRNA1-CHRNB1-CHRND-CHRNE)) (PubMed:35357806, PubMed:9174364). On mice muscle receptors, its higher affinity site is the alpha/delta nAChR subunit interface (PubMed:9174364). On Torpedo receptors, it does not distinguish between alpha/delta and alpha/gamma acetylcholine-binding sites (PubMed:9174364). In vivo, causes paralysis followed by death when injected into goldfish (PubMed:3196703). In contrast, has no effect on mice, when similar doses are intraperitoneally or intracerebrally injected (PubMed:3196703).<ref>PMID:3196703</ref> <ref>PMID:35357806</ref> <ref>PMID:9174364</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 14: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1qmw" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Barany, G.]]
+[[Category: Conus striatus]]
-[[Category: Benie, A J.]]
+[[Category: Large Structures]]
-[[Category: Hargittai, B.]]
+[[Category: Barany G]]
-[[Category: Janes, R W.]]
+[[Category: Benie AJ]]
-[[Category: Whitford, D.]]
+[[Category: Hargittai B]]
-[[Category: Conotoxin]]
+[[Category: Janes RW]]
-[[Category: Nicotinic acetylcholine receptor]]
+[[Category: Whitford D]]
-[[Category: Toxin]]
-[[Category: Venom]]

1qmw

From Proteopedia

Current revision

Solution structure of alpha-conotoxin SI

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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