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Figure 4
Magnification of the SHN3pS542 and SHN3pT869 peptides bound to 14-3-3σ. (a) The SHN3pS542 peptide is represented as purple sticks bound covalently through a disulfide bond to Cys38 of 14-3-3σ. 14-3-3σ is represented as a white surface and its Ser37, Cys38, Glu39 and Glu40 residues as grey sticks. The 2Fo − Fc map countered at σ = 1 is coloured blue for SHN3pS542 and grey for 14-3-3σ, suggesting the presence of a disulfide bond between Cys38 and Cys548. (b) Superposition of the SHN3pS542 and SHN3pT869 peptides bound to 14-3-3σ. The SHN3pS542 peptide (purple) occupies the entire 14-3-3σ groove, whereas the two consecutive prolines in SHN3pT869 cause the peptide to turn away from the 14-3-3 groove.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 77| Part 8| August 2021| Pages 254-261
https://doi.org/10.1107/S2053230X21006658
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