Inositol 1,4,5-Trisphosphate Receptor: Difference between revisions
Ann Taylor (talk | contribs) No edit summary |
Ann Taylor (talk | contribs) No edit summary |
||
| Line 1: | Line 1: | ||
[[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 <ref name="mainpaper">PMID:12442173</ref> | [[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 <ref name="mainpaper">PMID:12442173</ref> | ||
__NOTOC__ | __NOTOC__ | ||
==Structure== | ==Structure== | ||
<StructureSection load=' | <StructureSection load='1n4K' size='350' side='right' caption='Mouse inositol triphosphate receptor ligand-binding core complex with its ligand inositol triphosphate (PDB entry [[1n4K]])' scene=''> | ||
The specific type of inositol 1,4,5-trisphosphate receptor (InsP<sub>3</sub>R) protein discussed here is the mouse type 1 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.<ref name="mainpaper"/> The protein forms an L-shaped structure composed of two asymmetric domains perpendicular to each other.<ref name="mainpaper"/> The N-terminal domain is made up of 12 β-strands and 2 single-turn helices, which come together to form a barrel.<ref name="mainpaper"/> The C-terminal end is quite different, consisting of a bundle made of eight α-helices.<ref name="mainpaper"/> The interface of the two domains is lined with basic residues and forms the receptor site for InsP<sub>3</sub>.<ref name="mainpaper"/> The InsP<sub>3</sub>R protein does not belong to a superfamily of proteins. The receptor is thought to span the membrane 6 times, leaving the C-terminus in the cytoplasm.<ref name="functionref"/> | The specific type of inositol 1,4,5-trisphosphate receptor (InsP<sub>3</sub>R) protein discussed here is the mouse type 1 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.<ref name="mainpaper"/> The protein forms an L-shaped structure composed of two asymmetric domains perpendicular to each other.<ref name="mainpaper"/> The N-terminal domain is made up of 12 β-strands and 2 single-turn helices, which come together to form a barrel.<ref name="mainpaper"/> The C-terminal end is quite different, consisting of a bundle made of eight α-helices.<ref name="mainpaper"/> The interface of the two domains is lined with basic residues and forms the receptor site for InsP<sub>3</sub>.<ref name="mainpaper"/> The InsP<sub>3</sub>R protein does not belong to a superfamily of proteins. The receptor is thought to span the membrane 6 times, leaving the C-terminus in the cytoplasm.<ref name="functionref"/> | ||