Inositol 1,4,5-Trisphosphate Receptor
From Proteopedia
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<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- | + | 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 == |
| - | + | 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 inositol 1,4,5-trisphosphate (InsP<sub>3</sub>).<sup>[1]</sup> | |
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Revision as of 19:12, 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. |
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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 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 inositol 1,4,5-trisphosphate (InsP3).[1]
Proteopedia Page Contributors and Editors (what is this?)
Shannon King, Alexander Berchansky, Michal Harel, Ann Taylor, David Canner, Andrea Gorrell, Jaclyn Gordon
