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| [[Image:2dpr.gif|left|200px]]
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| {{Structure
| | ==The crystal structures of the calcium-bound con-G and con-T(K7Glu) dimeric peptides demonstrate a novel metal-dependent helix-forming motif== |
| |PDB= 2dpr |SIZE=350|CAPTION= <scene name='initialview01'>2dpr</scene>, resolution 1.7Å
| | <StructureSection load='2dpr' size='340' side='right'caption='[[2dpr]], [[Resolution|resolution]] 1.70Å' scene=''> |
| |SITE= | | == Structural highlights == |
| |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CGU:GAMMA-CARBOXY-GLUTAMIC+ACID'>CGU</scene>
| | <table><tr><td colspan='2'>[[2dpr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Conus_tulipa Conus tulipa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DPR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DPR FirstGlance]. <br> |
| |ACTIVITY=
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| |GENE=
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CGU:GAMMA-CARBOXY-GLUTAMIC+ACID'>CGU</scene></td></tr> |
| |DOMAIN=
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2dpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dpr OCA], [https://pdbe.org/2dpr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dpr RCSB], [https://www.ebi.ac.uk/pdbsum/2dpr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dpr ProSAT]</span></td></tr> |
| |RELATEDENTRY=[[2dpq|2DPQ]]
| | </table> |
| |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dpr OCA], [http://www.ebi.ac.uk/pdbsum/2dpr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2dpr RCSB]</span>
| | == Function == |
| }}
| | [https://www.uniprot.org/uniprot/CKT_CONTU CKT_CONTU] Conantokins inhibit N-methyl-D-aspartate (NMDA) receptors. This toxin inhibits both NR2A and NR2B subunits of N-methyl-D-aspartate (NMDA) receptor-mediated calcium influx in central nervous system neurons. Induces sleep-like symptoms in young mice and hyperactivity in older mice.<ref>PMID:2165278</ref> |
| | | == References == |
| '''The crystal structures of the calcium-bound con-G and con-T(K7Gla) dimeric peptides demonstrate a novel metal-dependent helix-forming motif'''
| | <references/> |
| | | __TOC__ |
| | | </StructureSection> |
| ==Overview== | | [[Category: Conus tulipa]] |
| Short peptides that have the ability to form stable alpha-helices in solution are rare, and a number of strategies have been used to produce them, including the use of metal chelation to stabilize folding of the backbone. However, no example exists of a structurally well-defined helix stabilized exclusively through metal ion chelation. Conantokins (con)-G and -T are short peptides that are potent antagonists of N-methyl-D-aspartate receptor channels. While con-G exhibits no helicity alone, it undergoes a structural transition to a helical conformation in the presence of a variety of multivalent cations, especially Mg2+ and Ca2+. This complexation also results in antiparallel dimerization of two peptide helices in the presence of Ca2+, but not Mg2+. A con-T variant, con-T[K7gamma], displays very similar behavior. We have solved the crystal structures of both Ca2+/con-G and Ca2+/con-T [K7gamma] at atomic resolution. These structures clearly show the nature of the metal-dependent dimerization and helix formation and surprisingly also show that the con-G dimer interface is completely different from the con-T[K7gamma] interface, even though the metal chelation is similar in the two peptides. This represents a new paradigm in helix stabilization completely independent of the hydrophobic effect, which we define as the "metallo-zipper."
| | [[Category: Large Structures]] |
| | | [[Category: Castellino FJ]] |
| ==About this Structure== | | [[Category: Cnudde SE]] |
| 2DPR is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DPR OCA].
| | [[Category: Dai Q]] |
| | | [[Category: Geiger JH]] |
| ==Reference==
| | [[Category: Prorok M]] |
| The crystal structures of the calcium-bound con-G and con-T[K7gamma] dimeric peptides demonstrate a metal-dependent helix-forming motif., Cnudde SE, Prorok M, Dai Q, Castellino FJ, Geiger JH, J Am Chem Soc. 2007 Feb 14;129(6):1586-93. Epub 2007 Jan 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17243678 17243678]
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| [[Category: Protein complex]] | |
| [[Category: Castellino, F J.]] | |
| [[Category: Cnudde, S E.]] | |
| [[Category: Dai, Q.]] | |
| [[Category: Geiger, J H.]] | |
| [[Category: Prorok, M.]] | |
| [[Category: con-t]]
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| [[Category: conantoxin]]
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| [[Category: gla-containing]]
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| [[Category: nmdar antagonist]]
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| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:37:44 2008''
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