This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2dpr
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2dpr.gif|left|200px]] | [[Image:2dpr.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2dpr", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_2dpr| PDB=2dpr | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''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''' | ||
| Line 19: | Line 16: | ||
==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.]] | ||
| Line 29: | Line 25: | ||
[[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
