1xzz

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1xzz, resolution 1.80Å

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Crystal structure of the ligand binding suppressor domain of type 1 inositol 1,4,5-trisphosphate receptor

Overview

Binding of inositol 1,4,5-trisphosphate (IP(3)) to the amino-terminal, region of IP(3) receptor promotes Ca(2+) release from the endoplasmic, reticulum. Within the amino terminus, the first 220 residues directly, preceding the IP(3) binding core domain play a key role in IP(3) binding, suppression and regulatory protein interaction. Here we present a crystal, structure of the suppressor domain of the mouse type 1 IP(3) receptor at, 1.8 A. Displaying a shape akin to a hammer, the suppressor region contains, a Head subdomain forming the beta-trefoil fold and an Arm subdomain, possessing a helix-turn-helix structure. The conserved region on the Head, subdomain appeared to interact with the IP(3) binding core domain and is, in close proximity to the previously proposed binding sites of Homer, RACK1, calmodulin, and CaBP1. The present study sheds light onto the, mechanism underlying the receptor's sensitivity to the ligand and its, communication with cellular signaling proteins.

About this Structure

1XZZ is a Single protein structure of sequence from Mus musculus with GOL as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of the ligand binding suppressor domain of type 1 inositol 1,4,5-trisphosphate receptor., Bosanac I, Yamazaki H, Matsu-Ura T, Michikawa T, Mikoshiba K, Ikura M, Mol Cell. 2005 Jan 21;17(2):193-203. PMID:15664189

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