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<StructureSection load="1pg1" size="400" color="" frame="true"  spin="on" Scene=  align="right" caption= >
<StructureSection load='1pg1' size='350' side='right' caption='NMR structure of pig protegrin 1, [[1pg1]]' scene=''>
[[Image:1pg1.png|left|200px]]
 
===PROTEGRIN 1 (PG1) FROM PORCINE LEUKOCYTES, NMR, 20 STRUCTURES===
 
{{ABSTRACT_PUBMED_8807886}}


__Toc__
==About this Structure==
==About this Structure==
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>.
'''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]
</StructureSection>
 
==3D structures of protegrin==
 
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
 
[[1pg1]], [[1zy6]] – pPRO1 – pig – NMR<BR />
[[2muh]] - pPRO2 residues 131-146 - NMR<br />
[[1n5h]], [[1n5p]] – pPRO3 cathelin-like domain – NMR<br />
[[1kwi]], [[1lxe]], [[1pfp]] – pPRO3 cathelin-like domain <br />
[[2m2z]], [[2mz6]] - pPRO3 residues 131-148 - NMR<br />
[[6qkf]] – pPRO4 residues 131-148 - NMR <br />
[[2nc7]] – pPRO5 residues 131-148 - NMR <br />
 
==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]
 
</StructureSection>
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Lehrer, R I.]]
[[Category: Lehrer, R I.]]
[[Category: Antimicrobial peptide]]
[[Category: Antimicrobial peptide]]


{{Reflist}}
{{Reflist}}
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Created with the participation of [[User:Lee Tien|Lee Tien]].
Created with the participation of [[User:Lee Tien|Lee Tien]].
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