Protegrin

About this Structure

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.

Gene Ontology^[5]

Cellular Component

• extracellular region (GO:0005576)

Biological Process

• defense response (GO:0006952)
• defense response to bacterium (GO:0042742)

SCOP Classification^[6]

• Fold: Antimicrobial beta-hairpin
• Superfamily: Antimicrobial beta-hairpin
• Family: theta defensin-like

3D structures of protegrin

Updated on 08-October-2020

1pg1, 1zy6 – pPRO1 – pig – NMR

2muh - pPRO2 residues 131-146 - NMR
1n5h, 1n5p – pPRO3 cathelin-like domain – NMR
1kwi, 1lxe, 1pfp – pPRO3 cathelin-like domain
2m2z, 2mz6 - pPRO3 residues 131-148 - NMR
6qkf – pPRO4 residues 131-148 - NMR
2nc7 – pPRO5 residues 131-148 - NMR

References

Solution structure of protegrin-1, a broad-spectrum antimicrobial peptide from porcine leukocytes., Fahrner RL, Dieckmann T, Harwig SS, Lehrer RI, Eisenberg D, Feigon J, Chem Biol. 1996 Jul;3(7):543-50. PMID:8807886