The STIM-Orai Pathway: STIM-Orai Structures: Isolated and in Complex View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

2017-09-13

AUTHORS

Jinhui Zhu , Qingping Feng , Peter B. Stathopulos

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. More... »

PAGES

15-38

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-3-319-57732-6_2

DOI

http://dx.doi.org/10.1007/978-3-319-57732-6_2

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1091608055

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/28900907


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