ContentsPROTEGRIN 1 (PG1) FROM PORCINE LEUKOCYTES, NMR, 20 STRUCTURESTemplate:ABSTRACT PUBMED 8807886 About this Structure1PG1 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. <StructureSection load="1pfp" size="400" color="" frame="true" spin="on" Scene= align="right" caption="Structure of pig proprotegrin 3 cathelin-like domain, 1pfp" > Gene Ontology[5]Cellular Component
Biological Process
SCOP Classification[6]
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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
Updated on 10-July-2013
1pg1, Single protein – pPRO1 – pig – NMR
1pfp, 1n5p – pPRO3 cathelin-like domain – NMR
1kwi, 1lxe, 1pfp – pPRO3 cathelin-like domain
Created with the participation of Lee Tien.
This page was last modified 10:05, 10 July 2013.
