Protegrin

spinqualitylabelsall models NMR structure of pig protegrin 1, 1pg1 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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. 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. The antimicrobial action of this protein is believed to be due to its ability to create pores in bacterial membranes causing ion leakage . This antimicrobial activity has given rise to the idea of using the peptide as a therapeutic for local or systemic infections. The protegrin is synthesized as a ca. 149 amino acid precursor with a cathelin-like domain. Gene Ontology Cellular Component extracellular region (GO:0005576) Biological Process defense response (GO:0006952) defense response to bacterium (GO:0042742) SCOP Classification Fold: Antimicrobial beta-hairpin Superfamily: Antimicrobial beta-hairpin Family: theta defensin-like

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

3D structures of protegrin

Updated on 14-July-2016

Single protein, 1zy6 – pPRO1 – pig – NMR
1n5h, 1n5p – pPRO3 cathelin-like domain – NMR
1kwi, 1lxe, 1pfp – pPRO3 cathelin-like domain

Created with the participation of Lee Tien.

Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Michal Harel, Jaime Prilusky