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.


2dpq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:25, 3 April 2024) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2dpq.gif|left|200px]]
 
-
<!--
+
==The crystal structures of the calcium-bound con-G and con-T(K7gamma) dimeric peptides demonstrate a novel metal-dependent helix-forming motif==
-
The line below this paragraph, containing "STRUCTURE_2dpq", creates the "Structure Box" on the page.
+
<StructureSection load='2dpq' size='340' side='right'caption='[[2dpq]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[2dpq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Conus_geographus Conus geographus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DPQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DPQ FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.25&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
-
{{STRUCTURE_2dpq| PDB=2dpq | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2dpq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dpq OCA], [https://pdbe.org/2dpq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dpq RCSB], [https://www.ebi.ac.uk/pdbsum/2dpq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dpq ProSAT]</span></td></tr>
-
 
+
</table>
-
'''The crystal structures of the calcium-bound con-G and con-T(K7gamma) dimeric peptides demonstrate a novel metal-dependent helix-forming motif'''
+
== Function ==
-
 
+
[https://www.uniprot.org/uniprot/CKG_CONGE 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.<ref>PMID:2165278</ref>
-
 
+
== References ==
-
==Overview==
+
<references/>
-
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."
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Conus geographus]]
-
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DPQ OCA].
+
[[Category: Large Structures]]
-
 
+
[[Category: Castellino FJ]]
-
==Reference==
+
[[Category: Cnudde SE]]
-
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: Dai Q]]
-
[[Category: Castellino, F J.]]
+
[[Category: Geiger JH]]
-
[[Category: Cnudde, S E.]]
+
[[Category: Prorok M]]
-
[[Category: Dai, Q.]]
+
-
[[Category: Geiger, J H.]]
+
-
[[Category: Prorok, M.]]
+
-
[[Category: Con-g]]
+
-
[[Category: Conantoxin]]
+
-
[[Category: Gla-containing]]
+
-
[[Category: Nmdar antagonist]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 00:55:38 2008''
+

Current revision

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

PDB ID 2dpq

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2dpq"
Personal tools