2a05

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:2a05.jpg|left|200px]]
[[Image:2a05.jpg|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 2a05 |SIZE=350|CAPTION= <scene name='initialview01'>2a05</scene>
+
The line below this paragraph, containing "STRUCTURE_2a05", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND=
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY=
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_2a05| PDB=2a05 | SCENE= }}
-
|RELATEDENTRY=
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a05 OCA], [http://www.ebi.ac.uk/pdbsum/2a05 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2a05 RCSB]</span>
+
-
}}
+
'''The cysteine-rich secretory protein domain of Tpx-1 is related to ion channel toxins and regulates Ryanodine receptor Ca2+ signaling'''
'''The cysteine-rich secretory protein domain of Tpx-1 is related to ion channel toxins and regulates Ryanodine receptor Ca2+ signaling'''
Line 34: Line 31:
[[Category: 3 alpha helice]]
[[Category: 3 alpha helice]]
[[Category: 5 disulphide bond]]
[[Category: 5 disulphide bond]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:26:40 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:46:08 2008''
+

Revision as of 15:26, 3 May 2008

Template:STRUCTURE 2a05

The cysteine-rich secretory protein domain of Tpx-1 is related to ion channel toxins and regulates Ryanodine receptor Ca2+ signaling


Overview

The cysteine-rich secretory proteins (Crisp) are predominantly found in the mammalian male reproductive tract as well as in the venom of reptiles. Crisps are two domain proteins with a structurally similar yet evolutionary diverse N-terminal domain and a characteristic cysteine-rich C-terminal domain, which we refer to as the Crisp domain. We presented the NMR solution structure of the Crisp domain of mouse Tpx-1, and we showed that it contains two subdomains, one of which has a similar fold to the ion channel regulators BgK and ShK. Furthermore, we have demonstrated for the first time that the ion channel regulatory activity of Crisp proteins is attributed to the Crisp domain. Specifically, the Tpx-1 Crisp domain inhibited cardiac ryanodine receptor (RyR) 2 with an IC(50) between 0.5 and 1.0 microM and activated the skeletal RyR1 with an AC(50) between 1 and 10 microM when added to the cytoplasmic domain of the receptor. This activity was nonvoltage-dependent and weakly voltage-dependent, respectively. Furthermore, the Tpx-1 Crisp domain activated both RyR forms at negative bilayer potentials and showed no effect at positive bilayer potentials when added to the luminal domain of the receptor. These data show that the Tpx-1 Crisp domain on its own can regulate ion channel activity and provide compelling evidence for a role for Tpx-1 in the regulation of Ca(2+) fluxes observed during sperm capacitation.

About this Structure

2A05 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

The cysteine-rich secretory protein domain of Tpx-1 is related to ion channel toxins and regulates ryanodine receptor Ca2+ signaling., Gibbs GM, Scanlon MJ, Swarbrick J, Curtis S, Gallant E, Dulhunty AF, O'Bryan MK, J Biol Chem. 2006 Feb 17;281(7):4156-63. Epub 2005 Dec 9. PMID:16339766 Page seeded by OCA on Sat May 3 18:26:40 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools