+Search query
-Structure paper
Title | Inositol 1,4,5-trisphosphate receptor contains multiple cavities and L-shaped ligand-binding domains. |
---|---|
Journal, issue, pages | J Mol Biol, Vol. 336, Issue 1, Page 155-164, Year 2004 |
Publish date | Feb 6, 2004 |
![]() | Chikara Sato / Kozo Hamada / Toshihiko Ogura / Atsuo Miyazawa / Kenji Iwasaki / Yoko Hiroaki / Kazutoshi Tani / Akiko Terauchi / Yoshinori Fujiyoshi / Katsuhiko Mikoshiba / ![]() |
PubMed Abstract | Calcium concentrations are strictly regulated in all biological cells, and one of the key molecules responsible for this regulation is the inositol 1,4,5-trisphosphate receptor, which was known to ...Calcium concentrations are strictly regulated in all biological cells, and one of the key molecules responsible for this regulation is the inositol 1,4,5-trisphosphate receptor, which was known to form a homotetrameric Ca(2+) channel in the endoplasmic reticulum. The receptor is involved in neuronal transmission via Ca(2+) signaling and for many other functions that relate to morphological and physiological processes in living organisms. We analysed the three-dimensional structure of the ligand-free form of the receptor based on a single-particle technique using an originally developed electron microscope equipped with a helium-cooled specimen stage and an automatic particle picking system. We propose a model that explains the complex mechanism for the regulation of Ca(2+) release by co-agonists, Ca(2+), inositol 1,4,5-trisphosphate based on the structure of multiple internal cavities and a porous balloon-shaped cytoplasmic domain containing a prominent L-shaped density which was assigned by the X-ray structure of the inositol 1,4,5-trisphosphate binding domain. |
![]() | ![]() ![]() |
Methods | EM (single particle) |
Resolution | 15.0 Å |
Structure data | ![]() EMDB-1061: |
Source |
|