Protegrin
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Created with the participation of Lee Tien.
ContentsAbout this StructureProtegrin 1 (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
Biological Process
SCOP Classification[6]
3D structures of protegrinUpdated on 30-July-2026 1pg1, 1zy6 – pPRO1 – pig – NMR 2mq2, 2mq4, 2mq5 – pPtn-1 (mutant) - NMR ReferencesSolution 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
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Created with the participation of Lee Tien.
This page was last modified 07:42, 30 July 2026.