1XZZ

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

Summary for 1XZZ

• Entry DOI: 10.2210/pdb1xzz/pdb
• Descriptor: Inositol 1,4,5-trisphosphate receptor type 1, GLYCEROL (3 entities in total)
• Functional Keywords: ip3 receptor, ip3 receptor suppressor domain, calcium channel, b-trefoil fold, membrane protein
• Biological source: Mus musculus (house mouse)
• Cellular location: Endoplasmic reticulum membrane; Multi-pass membrane protein: P11881
• Total number of polymer chains: 1
• Total formula weight: 27513.33

Authors

Bosanac, I.,Yamazaki, H.,Matsu-ura, T.,Michikawa, T.,Mikoshiba, K.,Ikura, M. (deposition date: 2004-11-13, release date: 2005-01-25, Last modification date: 2024-02-14)

Primary citation

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

PubMed Abstract: 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.

PubMed: 15664189
DOI: 10.1016/j.molcel.2004.11.047

Experimental method

X-RAY DIFFRACTION (1.8 Å)