1c6w: Difference between revisions

Latest revision as of 11:38, 22 November 2023

MAUROCALCIN FROM SCORPIO MAURUS

Structural highlights

1c6w is a 1 chain structure with sequence from Scorpio maurus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CAMAU_SCOPA This toxin stabilizes ryanodine receptor 1 (RyR1) opening in a long-lasting subconductance state (48%-60% of the full conductance state) (PubMed:10713267, PubMed:12869557, PubMed:27114612). Furthermore, it triggers calcium release from sarcoplasmic vesicles (6.6 nM are enough to induce a sharp release, and 60% of the total calcium is released after toxin (100 nM) addition) probably by acting as a cell-penetrating peptide (CPP) (PubMed:27114612). In addition, it has been shown to dose-dependently stimulate ryanodine binding to RyR1 (EC(50)=12.5-26.4 nM) (PubMed:12869557, PubMed:17291197, PubMed:17888395, PubMed:27114612). It also augments the bell-shaped calcium-[3H]ryanodine binding curve that is maximal at about 10 uM calcium concentration (PubMed:27114612). It binds a different site as ryanodine (PubMed:10713267). It acts synergistically with caffeine (By similarity). In vivo, intracerebroventricular injection into mice causes death (PubMed:10713267).[UniProtKB:A0A1L4BJ42][UniProtKB:B8QG00][UniProtKB:P59868]^[1] ^[2] ^[3] ^[4] ^[5]

Publication Abstract from PubMed

We determined the structure in solution by (1)H two-dimensional NMR of Maurocalcine from the venom of Scorpio maurus. This toxin has been demonstrated to be a potent effector of ryanodyne-sensitive calcium channel from skeletal muscles. This is the first description of a scorpion toxin which folds following the Inhibitor Cystine Knot fold (ICK) already described for numerous toxic and inhibitory peptides, as well as for various protease inhibitors. Its three dimensional structure consists of a compact disulfide-bonded core from which emerge loops and the N-terminus. A double-stranded antiparallel beta-sheet comprises residues 20-23 and 30-33. A third extended strand (residues 9-11) is perpendicular to the beta-sheet. Maurocalcine structure mimics the activating segment of the dihydropyridine receptor II-III loop and is therefore potentially useful for dihydropyridine receptor/ryanodine receptor interaction studies. Proteins 2000;40:436-442.

A new fold in the scorpion toxin family, associated with an activity on a ryanodine-sensitive calcium channel.,Mosbah A, Kharrat R, Fajloun Z, Renisio JG, Blanc E, Sabatier JM, El Ayeb M, Darbon H Proteins. 2000 Aug 15;40(3):436-42. PMID:10861934^[6]

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

References

↑ Fajloun Z, Kharrat R, Chen L, Lecomte C, Di Luccio E, Bichet D, El Ayeb M, Rochat H, Allen PD, Pessah IN, De Waard M, Sabatier JM. Chemical synthesis and characterization of maurocalcine, a scorpion toxin that activates Ca(2+) release channel/ryanodine receptors. FEBS Lett. 2000 Mar 10;469(2-3):179-85. PMID:10713267 doi:10.1016/s0014-5793(00)01239-4
↑ Estève E, Smida-Rezgui S, Sarkozi S, Szegedi C, Regaya I, Chen L, Altafaj X, Rochat H, Allen P, Pessah IN, Marty I, Sabatier JM, Jona I, De Waard M, Ronjat M. Critical amino acid residues determine the binding affinity and the Ca2+ release efficacy of maurocalcine in skeletal muscle cells. J Biol Chem. 2003 Sep 26;278(39):37822-31. PMID:12869557 doi:10.1074/jbc.M305798200
↑ Shahbazzadeh D, Srairi-Abid N, Feng W, Ram N, Borchani L, Ronjat M, Akbari A, Pessah IN, De Waard M, El Ayeb M. Hemicalcin, a new toxin from the Iranian scorpion Hemiscorpius lepturus which is active on ryanodine-sensitive Ca2+ channels. Biochem J. 2007 May 15;404(1):89-96. PMID:17291197 doi:10.1042/BJ20061404
↑ Mabrouk K, Ram N, Boisseau S, Strappazzon F, Rehaim A, Sadoul R, Darbon H, Ronjat M, De Waard M. Critical amino acid residues of maurocalcine involved in pharmacology, lipid interaction and cell penetration. Biochim Biophys Acta. 2007 Oct;1768(10):2528-40. PMID:17888395 doi:10.1016/j.bbamem.2007.06.030
↑ Xiao L, Gurrola GB, Zhang J, Valdivia CR, SanMartin M, Zamudio FZ, Zhang L, Possani LD, Valdivia HH. Structure-function relationships of peptides forming the calcin family of ryanodine receptor ligands. J Gen Physiol. 2016 May;147(5):375-94. PMID:27114612 doi:10.1085/jgp.201511499
↑ Mosbah A, Kharrat R, Fajloun Z, Renisio JG, Blanc E, Sabatier JM, El Ayeb M, Darbon H. A new fold in the scorpion toxin family, associated with an activity on a ryanodine-sensitive calcium channel. Proteins. 2000 Aug 15;40(3):436-42. PMID:10861934

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Fajloun Z, Kharrat R, Chen L, Lecomte C, Di Luccio E, Bichet D, El Ayeb M, Rochat H, Allen PD, Pessah IN, De Waard M, Sabatier JM. Chemical synthesis and characterization of maurocalcine, a scorpion toxin that activates Ca(2+) release channel/ryanodine receptors. FEBS Lett. 2000 Mar 10;469(2-3):179-85. PMID:10713267 doi:10.1016/s0014-5793(00)01239-4

[2] Estève E, Smida-Rezgui S, Sarkozi S, Szegedi C, Regaya I, Chen L, Altafaj X, Rochat H, Allen P, Pessah IN, Marty I, Sabatier JM, Jona I, De Waard M, Ronjat M. Critical amino acid residues determine the binding affinity and the Ca2+ release efficacy of maurocalcine in skeletal muscle cells. J Biol Chem. 2003 Sep 26;278(39):37822-31. PMID:12869557 doi:10.1074/jbc.M305798200

[3] Shahbazzadeh D, Srairi-Abid N, Feng W, Ram N, Borchani L, Ronjat M, Akbari A, Pessah IN, De Waard M, El Ayeb M. Hemicalcin, a new toxin from the Iranian scorpion Hemiscorpius lepturus which is active on ryanodine-sensitive Ca2+ channels. Biochem J. 2007 May 15;404(1):89-96. PMID:17291197 doi:10.1042/BJ20061404

[4] Mabrouk K, Ram N, Boisseau S, Strappazzon F, Rehaim A, Sadoul R, Darbon H, Ronjat M, De Waard M. Critical amino acid residues of maurocalcine involved in pharmacology, lipid interaction and cell penetration. Biochim Biophys Acta. 2007 Oct;1768(10):2528-40. PMID:17888395 doi:10.1016/j.bbamem.2007.06.030

[5] Xiao L, Gurrola GB, Zhang J, Valdivia CR, SanMartin M, Zamudio FZ, Zhang L, Possani LD, Valdivia HH. Structure-function relationships of peptides forming the calcin family of ryanodine receptor ligands. J Gen Physiol. 2016 May;147(5):375-94. PMID:27114612 doi:10.1085/jgp.201511499

[6] Mosbah A, Kharrat R, Fajloun Z, Renisio JG, Blanc E, Sabatier JM, El Ayeb M, Darbon H. A new fold in the scorpion toxin family, associated with an activity on a ryanodine-sensitive calcium channel. Proteins. 2000 Aug 15;40(3):436-42. PMID:10861934

[1]

[2]

[3]

[4]

[5]

[6]

@@ Line 1: / Line 1: @@
 ==MAUROCALCIN FROM SCORPIO MAURUS==
-<StructureSection load='1c6w' size='340' side='right'caption='[[1c6w]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>
+<StructureSection load='1c6w' size='340' side='right'caption='[[1c6w]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1c6w]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C6W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C6W FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1c6w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Scorpio_maurus Scorpio maurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C6W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C6W FirstGlance]. <br>
-</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=1c6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c6w OCA], [https://pdbe.org/1c6w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c6w RCSB], [https://www.ebi.ac.uk/pdbsum/1c6w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c6w ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1c6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c6w OCA], [https://pdbe.org/1c6w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c6w RCSB], [https://www.ebi.ac.uk/pdbsum/1c6w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c6w ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/CAMAU_SCOPA CAMAU_SCOPA] This toxin stabilizes ryanodine receptor 1 (RyR1) opening in a long-lasting subconductance state (48%-60% of the full conductance state) (PubMed:10713267, PubMed:12869557, PubMed:27114612). Furthermore, it triggers calcium release from sarcoplasmic vesicles (6.6 nM are enough to induce a sharp release, and 60% of the total calcium is released after toxin (100 nM) addition) probably by acting as a cell-penetrating peptide (CPP) (PubMed:27114612). In addition, it has been shown to dose-dependently stimulate ryanodine binding to RyR1 (EC(50)=12.5-26.4 nM) (PubMed:12869557, PubMed:17291197, PubMed:17888395, PubMed:27114612). It also augments the bell-shaped calcium-[3H]ryanodine binding curve that is maximal at about 10 uM calcium concentration (PubMed:27114612). It binds a different site as ryanodine (PubMed:10713267). It acts synergistically with caffeine (By similarity). In vivo, intracerebroventricular injection into mice causes death (PubMed:10713267).[UniProtKB:A0A1L4BJ42][UniProtKB:B8QG00][UniProtKB:P59868]<ref>PMID:10713267</ref> <ref>PMID:12869557</ref> <ref>PMID:17291197</ref> <ref>PMID:17888395</ref> <ref>PMID:27114612</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 23: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Ayeb, M]]
+[[Category: Scorpio maurus]]
-[[Category: Blanc, E]]
+[[Category: Ayeb M]]
-[[Category: Darbon, H]]
+[[Category: Blanc E]]
-[[Category: Fajloun, Z]]
+[[Category: Darbon H]]
-[[Category: Kharrat, R]]
+[[Category: Fajloun Z]]
-[[Category: Mosbah, A]]
+[[Category: Kharrat R]]
-[[Category: Renisio, J G]]
+[[Category: Mosbah A]]
-[[Category: Sabatier, J M]]
+[[Category: Renisio J-G]]
-[[Category: Ryanodine receptor effector]]
+[[Category: Sabatier J-M]]
-[[Category: Scorpion toxin]]
-[[Category: Toxin]]

1c6w: Difference between revisions

Latest revision as of 11:38, 22 November 2023

MAUROCALCIN FROM SCORPIO MAURUS

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools