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Adv Exp Med Biol. 2017;993:15-38. doi: 10.1007/978-3-319-57732-6_2.

The STIM-Orai Pathway: STIM-Orai Structures: Isolated and in Complex.

Author information

1
Department of Physiology and Pharmacology, Schulich School of Medicine and Dentistry, Western University, London, ON, Canada, N6A 5C1.
2
Department of Physiology and Pharmacology, Schulich School of Medicine and Dentistry, Western University, London, ON, Canada, N6A 5C1. peter.stathopulos@schulich.uwo.ca.

Abstract

Considerable progress has been made elucidating the molecular mechanisms of calcium (Ca2+) sensing by stromal interaction molecules (STIMs) and the basis for Orai channel activity. This chapter focuses on the available high-resolution structural details of STIM and Orai proteins with respect to the regulation of store-operated Ca2+ entry (SOCE). Solution structures of the Ca2+-sensing domains of STIM1 and STIM2 are reviewed in detail, crystal structures of cytosolic coiled-coil STIM fragments are discussed, and an overview of the closed Drosophila melanogaster Orai hexameric structure is provided. Additionally, we highlight structures of human Orai1 N-terminal and C-terminal domains in complex with calmodulin and human STIM1, respectively. Ultimately, the accessible structural data are discussed in terms of potential mechanisms of action and cohesiveness with functional observations.

KEYWORDS:

Calmodulin; Orai1; Solution nuclear magnetic resonance spectroscopy; Store-operated calcium entry; Stromal interaction molecules; Structural mechanisms; X-ray crystallography

PMID:
28900907
DOI:
10.1007/978-3-319-57732-6_2
[Indexed for MEDLINE]

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