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Figure 2
Thermal-shift assay of GLP-1R mutants, and potential mechanisms of I1962.66bF and S2714.47bA in the thermal stability and crystallization of GLP-1R. (a) SEC of GLP-1R fusion proteins suggests that the GLP-1R mutants are mostly monomeric and of similar homogeneity. (b) Thermal-shift assay of GLP-1R mutants in apo state or in complex with ligand PF-06372222. The different melting temperatures of the GLP-1R mutants indicating these mutations significantly affect thermal stability. (c) Densities of representative mutations in mutant structures. (d) B factor and distribution map of four constructs. (e) I1962.66bF mutation stabilized GLP-1R through its connections with the central polar network and other regions. (f) Packing and asymmetric unit of the four crystallized constructs. The back mutation of A2714.47bS induced significant change in the cell contents of M6 (yellow) compared with the other three back mutations and disturbed the packing. The four structures are superimposed through chain b. In Figs. 2[link](e) and 2[link](f) the color codes are shown in the key at the center.

Volume 6| Part 6| November 2019| Pages 996-1006
ISSN: 2052-2525