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. 2022 Jun 3;119(23):e2200794119. doi: 10.1073/pnas.2200794119

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Copyright © 2022 the Author(s). Published by PNAS.

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Fig. 2. — Myristoyl swap. (A) Cartoon representation of myrMA₁₁₂ chain b showing the dimeric interface formed by two trimers through a myr swapping mode (cyan and magenta). The two trimers are aligned in an antiparallel mode. (B) Cartoon representation showing two myrMA₁₁₂ molecules (cyan and magenta) in which the myr group (red) is sequestered in a preexisting hydrophobic cavity of an adjacent molecule. For comparison, the NMR structure of the monomeric myrMA protein (gray; PDB ID code 2H3I) is shown with the myr group buried in an identical hydrophobic cavity formed by the side chains of residues Trp16, Ile34, Leu51, Leu85, and Val88.