Protegrin

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==About this Structure==
==About this Structure==
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1PG1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PG1 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 [http://proteopedia.org/wiki/index.php/1zy6 1ZY6]. The structure of 1PG1 is similar to that of some other [http://en.wikipedia.org/wiki/Antimicrobial_peptide antimicrobial peptides] such as [http://en.wikipedia.org/wiki/Defensin defensins]<ref>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: [http://www.ncbi.nlm.nih.gov/pubmed/2668334 2668334]</ref>. In one study comparing the susceptibility of [http://en.wikipedia.org/wiki/Chlamydia_trachomatis Chlamydia trachomatis] to 1PG1 and a similar defensin peptide, 1PG1 was shown to be significantly more effective at inactivating the bacteria<ref>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: [http://www.ncbi.nlm.nih.gov/pubmed/8641770 8641770]</ref>. The antimicrobial action of this protein is believed to be due to its ability to create pores in bacterial membranes causing ion leakage <ref>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:[http://www.ncbi.nlm.nih.gov/pubmed/10446287 10446287]</ref>. This antimicrobial activity has given rise to the idea of using the peptide as a therapeutic for local or systemic infections<ref>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: [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC163996/ PMC163996]</ref>. The protegrin is synthesized as a ca. 149 amino acid precursor with a cathelin-like domain.
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'''Protegrin 1''' (1PG1) is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PG1 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 [http://proteopedia.org/wiki/index.php/1zy6 1ZY6]. The structure of 1PG1 is similar to that of some other [http://en.wikipedia.org/wiki/Antimicrobial_peptide antimicrobial peptides] such as [http://en.wikipedia.org/wiki/Defensin defensins]<ref>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: [http://www.ncbi.nlm.nih.gov/pubmed/2668334 2668334]</ref>. In one study comparing the susceptibility of [http://en.wikipedia.org/wiki/Chlamydia_trachomatis Chlamydia trachomatis] to 1PG1 and a similar defensin peptide, 1PG1 was shown to be significantly more effective at inactivating the bacteria<ref>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: [http://www.ncbi.nlm.nih.gov/pubmed/8641770 8641770]</ref>. The antimicrobial action of this protein is believed to be due to its ability to create pores in bacterial membranes causing ion leakage <ref>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:[http://www.ncbi.nlm.nih.gov/pubmed/10446287 10446287]</ref>. This antimicrobial activity has given rise to the idea of using the peptide as a therapeutic for local or systemic infections<ref>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: [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC163996/ PMC163996]</ref>. The protegrin is synthesized as a ca. 149 amino acid precursor with a cathelin-like domain.
==Gene Ontology<ref>NPG1. EBI QuickGO. [http://www.ebi.ac.uk/QuickGO/GProtein?ac=P32194 http://www.ebi.ac.uk/QuickGO/GProtein?ac=P32194]</ref>==
==Gene Ontology<ref>NPG1. EBI QuickGO. [http://www.ebi.ac.uk/QuickGO/GProtein?ac=P32194 http://www.ebi.ac.uk/QuickGO/GProtein?ac=P32194]</ref>==
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*'''Superfamily:''' [http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.ba.e.b.html Antimicrobial beta-hairpin]
*'''Superfamily:''' [http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.ba.e.b.html Antimicrobial beta-hairpin]
*'''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]
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</StructureSection>
 
==3D structures of protegrin==
==3D structures of protegrin==
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==References==
==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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</StructureSection>
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]

Current revision

NMR structure of pig protegrin 1, 1pg1

Drag the structure with the mouse to rotate


  1. 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
  2. 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
  3. 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
  4. 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
  5. NPG1. EBI QuickGO. http://www.ebi.ac.uk/QuickGO/GProtein?ac=P32194
  6. 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


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