2dpr

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|PDB= 2dpr |SIZE=350|CAPTION= <scene name='initialview01'>2dpr</scene>, resolution 1.7&Aring;
|PDB= 2dpr |SIZE=350|CAPTION= <scene name='initialview01'>2dpr</scene>, resolution 1.7&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CGU:GAMMA-CARBOXY-GLUTAMIC+ACID'>CGU</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=[[2dpq|2DPQ]]
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|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>
}}
}}
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[[Category: Geiger, J H.]]
[[Category: Geiger, J H.]]
[[Category: Prorok, M.]]
[[Category: Prorok, M.]]
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[[Category: CA]]
 
[[Category: con-t]]
[[Category: con-t]]
[[Category: conantoxin]]
[[Category: conantoxin]]
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[[Category: nmdar antagonist]]
[[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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:37:44 2008''

Revision as of 23:37, 30 March 2008


PDB ID 2dpr

Drag the structure with the mouse to rotate
, resolution 1.7Å
Ligands: ,
Related: 2DPQ


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



The crystal structures of the calcium-bound con-G and con-T(K7Gla) dimeric peptides demonstrate a novel metal-dependent helix-forming motif


Overview

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."

About this Structure

2DPR is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.

Reference

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:17243678

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