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. Author manuscript; available in PMC: 2015 Jul 16.
Published in final edited form as: J Mol Biol. 2014 Oct 2;427(1):77–93. doi: 10.1016/j.jmb.2014.09.021

Figure 3. Structural features of the STIM1 C-terminus.

Figure 3

A) Schematic of the human SOAR crystal structure (PDB ID code 3TEQ). The two monomers (gray and violet) form a parallel dimer, with interactions between the CC2 and CC3 of each monomer. B) Schematic of the C.elegans STIM crystal structure (PDB ID code 3TER) encompassing domains CC1-CC3. In C. elegans, the CC2 and CC3 domains and dimer arrangements are similar to the human SOAR structure (monomers shown in blue and pink). C) NMR structure of STIM1 encompassing amino acids 312–387 (PDB ID code 2MAJ). The two monomers in yellow and green are arranged in anti-parallel manner. CC2 (yellow) interacts with CC2’ (green) of the other monomer, likewise CC1 (yellow) associates with CC1’(green). This structure is displayed vertically on its long axis for easier comparison with the two crystal structures. D) Solution structure of the complex between STIM1312–387 and Orai1272–292 (PDB ID code 2MAK). The STIM1312–387 monomers (cyan and blue) are anti-parallel, and the two identical CC2:CC2’ interfaces form composite binding surfaces for the two Orai1 C272–292 (magenta) fragments. Homotypic interactions of CC1:CC1’ are also observed. The model figures were generated using PyMOL.