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1pen

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ALPHA-CONOTOXIN PNI1

Structural highlights

1pen is a 1 chain structure with sequence from Conus pennaceus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.1Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CA1A_CONPE Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin blocks mammalian nAChRs (alpha-3/beta-2 > alpha-7 > alpha-3/beta-4).^[1] ^[2]

Publication Abstract from PubMed

BACKGROUND: alpha-Conotoxins are peptide toxins, isolated from Conus snails, that block the nicotinic acetylcholine receptor (nAChR). The 16-residue peptides PnIA and PnIB from Conus pennaceus incorporate the same disulfide framework as other alpha-conotoxins but differ in function from most alpha-conotoxins by blocking the neuronal nAChR, rather than the skeletal muscle subtype. The crystal structure determination of PnIA was undertaken to identify structural and surface features that might be important for biological activity. RESULTS: The 1.1 A crystal structure of synthetic PnIA was determined by direct methods using the Shake-and-Bake program. The three-dimensional structure incorporates a beta turn followed by two alpha-helical turns. The conformation is stabilised by two disulfide bridges that form the interior of the molecule, with all other side chains oriented outwards. CONCLUSIONS: The compact architecture of the PnIA toxin provides a rigid framework for presentation of chemical groups that are required for activity. The structure is characterized by distinct hydrophobic and polar surfaces; a 16 A separation of the sole positive and negative charges (these two charged residues being located at opposite ends of the molecule); a hydrophobic region and a protruding tyrosine side chain. These features may be important for the specific interaction of PnIA with neuronal nAChR.

The 1.1 A crystal structure of the neuronal acetylcholine receptor antagonist, alpha-conotoxin PnIA from Conus pennaceus.,Hu SH, Gehrmann J, Guddat LW, Alewood PF, Craik DJ, Martin JL Structure. 1996 Apr 15;4(4):417-23. PMID:8740364^[3]

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

References

↑ Luo S, Nguyen TA, Cartier GE, Olivera BM, Yoshikami D, McIntosh JM. Single-residue alteration in alpha-conotoxin PnIA switches its nAChR subtype selectivity. Biochemistry. 1999 Nov 2;38(44):14542-8. PMID:10545176
↑ Fainzilber M, Hasson A, Oren R, Burlingame AL, Gordon D, Spira ME, Zlotkin E. New mollusc-specific alpha-conotoxins block Aplysia neuronal acetylcholine receptors. Biochemistry. 1994 Aug 16;33(32):9523-9. PMID:8068627
↑ Hu SH, Gehrmann J, Guddat LW, Alewood PF, Craik DJ, Martin JL. The 1.1 A crystal structure of the neuronal acetylcholine receptor antagonist, alpha-conotoxin PnIA from Conus pennaceus. Structure. 1996 Apr 15;4(4):417-23. PMID:8740364

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/1pen"

@@ Line 1: / Line 1: @@
 ==ALPHA-CONOTOXIN PNI1==
-<StructureSection load='1pen' size='340' side='right' caption='[[1pen]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
+<StructureSection load='1pen' size='340' side='right'caption='[[1pen]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1pen]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Conus_pennaceus Conus pennaceus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PEN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PEN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1pen]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Conus_pennaceus Conus pennaceus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PEN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PEN 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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.1&#8491;</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=1pen FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pen OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1pen RCSB], [http://www.ebi.ac.uk/pdbsum/1pen 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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pen FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pen OCA], [https://pdbe.org/1pen PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pen RCSB], [https://www.ebi.ac.uk/pdbsum/1pen PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pen ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CXAA_CONPE CXAA_CONPE]] Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin blocks mammalian nAChRs (alpha-3/beta-2 > alpha-7 > alpha-3/beta-4).<ref>PMID:8068627</ref> <ref>PMID:10545176</ref>
+[https://www.uniprot.org/uniprot/CA1A_CONPE CA1A_CONPE] Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin blocks mammalian nAChRs (alpha-3/beta-2 > alpha-7 > alpha-3/beta-4).<ref>PMID:10545176</ref> <ref>PMID:8068627</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 16: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1pen" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
@@ Line 21: / Line 24: @@
 </StructureSection>
 [[Category: Conus pennaceus]]
-[[Category: Alewood, P F]]
+[[Category: Large Structures]]
-[[Category: Craik, D J]]
+[[Category: Alewood PF]]
-[[Category: Gehrmann, J]]
+[[Category: Craik DJ]]
-[[Category: Guddat, L W]]
+[[Category: Gehrmann J]]
-[[Category: Hu, S H]]
+[[Category: Guddat LW]]
-[[Category: Martin, J L]]
+[[Category: Hu S-H]]
-[[Category: Acetylcholine receptor]]
+[[Category: Martin JL]]
-[[Category: Acetylcholine receptor inhibitor]]
-[[Category: Antagonist]]
-[[Category: Neurotoxin]]
-[[Category: Postsynaptic]]

1pen

From Proteopedia

Current revision

ALPHA-CONOTOXIN PNI1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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