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. 2021 Feb 22;12:597951. doi: 10.3389/fimmu.2021.597951

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Copyright © 2021 Merselis, Rivas and Munson

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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The P2 domain of murine Perforin-2. The most prominent feature within the P2 domain is an extended β-hairpin; highlighted in dark orange. Two disulfide bonds stiffen the β-hairpin. Hydrophobic residues at the β-hairpin’s tip are shown in dark green. These residues likely orient Perforin-2 on phagocytosed bacteria by initiating contact with target lipid bilayers. Numbering is relative to UniProt accession number A1L314. This graphic was rendered with UCSF Chimera from PDB file 6SB1 (http://www.rcsb.org/structure/6SB1) (20).