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.
Inositol 1,4,5-Trisphosphate Receptor
From Proteopedia
| Line 3: | Line 3: | ||
| - | <scene name='Sandbox_170/1n4k/4'>Inositol 1,4,5- | + | <scene name='Sandbox_170/1n4k/4'>Inositol 1,4,5-trisphosphate receptor</scene> |
<applet load='1n4k' size='300' frame='true' align='right' caption='Inositol 1,4,5-triphosphate receptor' /> | <applet load='1n4k' size='300' frame='true' align='right' caption='Inositol 1,4,5-triphosphate receptor' /> | ||
Inositol 1,4,5-trisphosphate receptor binding protein is a ubiquitous protein involved in the Ca<sup>2+</sup> signalling processes in a variety of organisms <sup>[1]</sup> | Inositol 1,4,5-trisphosphate receptor binding protein is a ubiquitous protein involved in the Ca<sup>2+</sup> signalling processes in a variety of organisms <sup>[1]</sup> | ||
== Structure == | == Structure == | ||
| - | The protein forms an L-shaped structure composed of two asymmetric domains perpendicular to each other.<sup>[1]</sup> The N-terminal domain is made up of 12 β-strands and 2 single-turn helices.<sup>[1]</sup> These components form a barrel. The C-terminal end is quite different, consisting of a bundle made of eight α-helices.<sup>[1]</sup> The interface of the two domains is lined with basic residues and forms the receptor site for | + | The specific type of inositol 1,4,5-trisphosphate receptor (InsP<sub>3</sub>R)protein discussed here is the mouse type one InsP<sub>3</sub>R, also called InsP<sub>3</sub>R1. This polypeptide contains three major regions: the amino terminal inositol 1,4,5-trisphosphate (InsP<sub>3</sub>) binding region, the central modulatory region, and the carboxy-terminus channel region.<sup>1</sup> The protein forms an L-shaped structure composed of two asymmetric domains perpendicular to each other.<sup>[1]</sup> The N-terminal domain is made up of 12 β-strands and 2 single-turn helices.<sup>[1]</sup> These components form a barrel. The C-terminal end is quite different, consisting of a bundle made of eight α-helices.<sup>[1]</sup> The interface of the two domains is lined with basic residues and forms the receptor site for InsP<sub>3</sub>.<sup>[1]</sup> |
---- | ---- | ||
Revision as of 20:44, 16 March 2010
| Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. Andrea Gorrell. |
|
Inositol 1,4,5-trisphosphate receptor binding protein is a ubiquitous protein involved in the Ca2+ signalling processes in a variety of organisms [1]
Structure
The specific type of inositol 1,4,5-trisphosphate receptor (InsP3R)protein discussed here is the mouse type one InsP3R, also called InsP3R1. This polypeptide contains three major regions: the amino terminal inositol 1,4,5-trisphosphate (InsP3) binding region, the central modulatory region, and the carboxy-terminus channel region.1 The protein forms an L-shaped structure composed of two asymmetric domains perpendicular to each other.[1] The N-terminal domain is made up of 12 β-strands and 2 single-turn helices.[1] These components form a barrel. The C-terminal end is quite different, consisting of a bundle made of eight α-helices.[1] The interface of the two domains is lined with basic residues and forms the receptor site for InsP3.[1]
Proteopedia Page Contributors and Editors (what is this?)
Shannon King, Alexander Berchansky, Michal Harel, Ann Taylor, David Canner, Andrea Gorrell, Jaclyn Gordon
