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Protegrin
From Proteopedia
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*'''Family:''' [http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.ba.e.b.f.html theta defensin-like] | *'''Family:''' [http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.ba.e.b.f.html 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:[http://www.ncbi.nlm.nih.gov/pubmed/8807886 8807886] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8807886 8807886] | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
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{{Reflist}} | {{Reflist}} | ||
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| + | Created with the participation of [[User:Lee Tien|Lee Tien]]. | ||
Revision as of 08:24, 5 June 2012
Contents |
PROTEGRIN 1 (PG1) FROM PORCINE LEUKOCYTES, NMR, 20 STRUCTURES
Template:ABSTRACT PUBMED 8807886
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].
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
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
- ↑ 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
- ↑ NPG1. EBI QuickGO. http://www.ebi.ac.uk/QuickGO/GProtein?ac=P32194
- ↑ Protein: Protegrin 1 (PG1) from Pig (Sus scrofa). Structural Classification of Proteins. http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.ba.e.b.f.b.html
Created with the participation of Lee Tien.
