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Figure 3
Alternative conformations of P3 and P4 residues. Protease residues from chain A are shown in white, those from chain B in gray and substrates in black. (a) The CA/p2 complex (PDB entry 1f7a). Ala2 (P4) and Arg3 (P3) form β-sheet-like interchain hydrogen bonds to Asp29 and Gly48. (b) The p1/p6 complex (PDB entry 1kjf). Gly48 and Arg8 alternatively recognize the P3/P4 amide. (c) The alternative orientations A and B of SGIFLETS exhibit the conserved β-sheet conformation and a unique hydrogen bond between the side chains of Ser1A/B (P4) and Lys45. (d) Alternative conformation C is similar to that in (b) and has a unique hydrogen bond between the side-chain hydroxyl group of Ser1C (P4) and the main-chain O atom of Gly49.

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
Volume 74| Part 7| July 2018| Pages 690-694
https://doi.org/10.1107/S2059798318006691
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