2dpr
From Proteopedia
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[[Image:2dpr.gif|left|200px]] | [[Image:2dpr.gif|left|200px]] | ||
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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''' | '''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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==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DPR OCA]. | |
==Reference== | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/17243678 17243678] | 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] | ||
| - | [[Category: Protein complex]] | ||
[[Category: Castellino, F J.]] | [[Category: Castellino, F J.]] | ||
[[Category: Cnudde, S E.]] | [[Category: Cnudde, S E.]] | ||
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[[Category: Geiger, J H.]] | [[Category: Geiger, J H.]] | ||
[[Category: Prorok, M.]] | [[Category: Prorok, M.]] | ||
| - | [[Category: | + | [[Category: Con-t]] |
| - | [[Category: | + | [[Category: Conantoxin]] |
| - | [[Category: | + | [[Category: Gla-containing]] |
| - | [[Category: | + | [[Category: Nmdar antagonist]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 00:55:46 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 21:55, 3 May 2008
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
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 Page seeded by OCA on Sun May 4 00:55:46 2008
