2dpq: Difference between revisions
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|PDB= 2dpq |SIZE=350|CAPTION= <scene name='initialview01'>2dpq</scene>, resolution 1.25Å | |PDB= 2dpq |SIZE=350|CAPTION= <scene name='initialview01'>2dpq</scene>, resolution 1.25Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CGU:GAMMA-CARBOXY-GLUTAMIC+ACID'>CGU</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2dpr|2DPR]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dpq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dpq OCA], [http://www.ebi.ac.uk/pdbsum/2dpq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2dpq RCSB]</span> | |||
}} | }} | ||
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[[Category: Geiger, J H.]] | [[Category: Geiger, J H.]] | ||
[[Category: Prorok, M.]] | [[Category: Prorok, M.]] | ||
[[Category: con-g]] | [[Category: con-g]] | ||
[[Category: conantoxin]] | [[Category: conantoxin]] | ||
| Line 33: | Line 34: | ||
[[Category: nmdar antagonist]] | [[Category: nmdar antagonist]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:37:48 2008'' | ||
Revision as of 23:37, 30 March 2008
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| 2dpq, resolution 1.25Å | |||||||||||||
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| Ligands: | CA, CGU, CL, NH2 | ||||||||||||
| Related: | 2DPR
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
The crystal structures of the calcium-bound con-G and con-T(K7gamma) 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
2DPQ 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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