 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 3]](ag5041fig3mag.jpg)
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Figure 3
Crystal structures of 14-3-3σ in complex with the phosphorylated peptides SHN3pS542 and SHN3pT869. (a, b) Surface representations of the asymmetric units of the 14-3-3σ–SHN3pS542 and 14-3-3σ–SHN3pT869 crystal structures. The 14-3-3σ monomer is represented as a white surface with transparency at 60% and as a white cartoon highlighting the secondary structure of 14-3-3 proteins: nine α-helices and loops that connect them. The SHN3pS542 peptide is represented as purple spheres and the SHN3pT869 peptide is represented as orange spheres. (c, d) Stick representation of the SHN3pS542 peptide (purple) and SHN3pT869 peptide (orange) bound to the 14-3-3σ amphipathic binding groove. Polar bonds are represented as dotted black lines. (e, f) Stick representation of the SHN3pS542 peptide (purple) and the SHN3pT869 peptide (orange) with their 2Fo − Fc maps contoured at σ = 1. The side chain of Arg539 of the SHN3pS542 peptide has not been modelled due to the lack of electron density in this area. |
![[Figure 3]](ag5041fig3.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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