2dpq

The crystal structures of the calcium-bound con-G and con-T(K7gamma) dimeric peptides demonstrate a novel metal-dependent helix-forming motif

spinqualitylabelsall models 2dpq, resolution 1.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2dpq is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, CL NonStd Res: CGU, NH2 Related: 2dpr Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CKG_CONGE] Conantokins inhibit N-methyl-D-aspartate (NMDA) receptors. This toxin is selective for the NR2B/GRIN2B subunit. Induces sleep-like symptoms in young mice and hyperactivity in older mice. Publication Abstract from PubMed 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." 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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