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2dpr

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[[Image:2dpr.gif|left|200px]]
 
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{{Structure
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==The crystal structures of the calcium-bound con-G and con-T(K7Glu) dimeric peptides demonstrate a novel metal-dependent helix-forming motif==
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|PDB= 2dpr |SIZE=350|CAPTION= <scene name='initialview01'>2dpr</scene>, resolution 1.7&Aring;
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<StructureSection load='2dpr' size='340' side='right'caption='[[2dpr]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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<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>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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|GENE=
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<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>
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}}
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<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>
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</table>
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'''The crystal structures of the calcium-bound con-G and con-T(K7Gla) dimeric peptides demonstrate a novel metal-dependent helix-forming motif'''
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== Function ==
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[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>
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== References ==
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==Overview==
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<references/>
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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."
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Conus tulipa]]
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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].
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[[Category: Large Structures]]
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[[Category: Castellino FJ]]
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==Reference==
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[[Category: Cnudde SE]]
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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: Dai Q]]
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[[Category: Protein complex]]
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[[Category: Geiger JH]]
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[[Category: Castellino, F J.]]
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[[Category: Prorok M]]
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[[Category: Cnudde, S E.]]
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[[Category: Dai, Q.]]
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[[Category: Geiger, J H.]]
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[[Category: Prorok, M.]]
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[[Category: CA]]
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[[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 Thu Mar 20 16:29:59 2008''
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Current revision

The crystal structures of the calcium-bound con-G and con-T(K7Glu) dimeric peptides demonstrate a novel metal-dependent helix-forming motif

PDB ID 2dpr

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