Inositol 1,4,5-Trisphosphate Receptor: Difference between revisions
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{{STRUCTURE_1n4k | PDB=1n4k | SCENE= }} | {{STRUCTURE_1n4k | PDB=1n4k | SCENE= }} | ||
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> | ||
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== Overall Structure == | == Overall Structure == | ||
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"/> | ||