1PG1 is a Single protein structure of sequence from Sus scrofa. Full experimental information is available from OCA. 1PG1 is an arginine and cysteine rich protein, which forms a double stranded anti-parallel β-sheet structure. The single chain forms a membrane-bound dimer, of structure 1ZY6. The structure of 1PG1 is similar to that of some other antimicrobial peptides such as defensins[1]. In one study comparing the susceptibility of Chlamydia trachomatis to 1PG1 and a similar defensin peptide, 1PG1 was shown to be significantly more effective at inactivating the bacteria[2]. The antimicrobial action of this protein is believed to be due to its ability to create pores in bacterial membranes causing ion leakage [3]. This antimicrobial activity has given rise to the idea of using the peptide as a therapeutic for local or systemic infections[4]. The protegrin is synthesized as a ca. 149 amino acid precursor with a cathelin-like domain.
↑Interaction of human defensins with Escherichia coli. Mechanism of bactericidal activity., Lehrer RI, Barton A, Daher KA, Harwig SS, Ganz T, Selsted ME., J Clin Invest. 1989 Aug;84(2):553-61. PMID: 2668334
↑Susceptibility of Chlamydia trachomatis to protegrins and defensins., Yasin B, Harwig SS, Lehrer RI, Wagar EA., Infect Immun. 1996 Mar;64(3):709-13. PMID: 8641770
↑Membrane channel formation by antimicrobial protegrins., Sokolov Y, Mirzabekov T, Martin DW, Lehrer RI, Kagan BL, Biochim Biophys Acta. 1999 Aug 20;1420(1-2):23-9. PMID:10446287
↑Protegrin-1: a broad-spectrum, rapidly microbicidal peptide with in vivo activity, D A Steinberg, M A Hurst, C A Fujii, A H Kung, J F Ho, F C Cheng, D J Loury, and J C Fiddes, Antimicrob Agents Chemother. 1997 August; 41(8): 1738–1742. PMCID: PMC163996
