2g9l
From Proteopedia
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'''The High-resolution Solution Conformation of an Antimicrobial Peptide Gaegurin 4 and Its Mode of Membrane Interaction'''<br /> | '''The High-resolution Solution Conformation of an Antimicrobial Peptide Gaegurin 4 and Its Mode of Membrane Interaction'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We have applied NMR spectroscopy to determine the high-resolution | + | We have applied NMR spectroscopy to determine the high-resolution structure of gaegurin 4, a 37-residue antimicrobial peptide from Rana rugosa, under varying hydrophobic conditions. Even in 100% H2O, gaegurin 4 contains a nascent turn near its C-terminal Rana box. Under a more hydrophobic condition it forms two amphipathic helices, one long encompassing residues 2-23 and the other consisting of residues 25-34, similar to what has been observed in cecropin A. Functional implication of the helix-breaking kink at Gly24 in gaegurin 4 was investigated by preparing several analogs. Based upon the current and previous results, we propose a novel seaanemone-like ion pore-forming model for gaegurin 4. |
==About this Structure== | ==About this Structure== | ||
| - | 2G9L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 2G9L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G9L OCA]. |
==Reference== | ==Reference== | ||
Solution structure and membrane interaction mode of an antimicrobial peptide gaegurin 4., Chi SW, Kim JS, Kim DH, Lee SH, Park YH, Han KH, Biochem Biophys Res Commun. 2007 Jan 19;352(3):592-7. Epub 2006 Nov 27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17141187 17141187] | Solution structure and membrane interaction mode of an antimicrobial peptide gaegurin 4., Chi SW, Kim JS, Kim DH, Lee SH, Park YH, Han KH, Biochem Biophys Res Commun. 2007 Jan 19;352(3):592-7. Epub 2006 Nov 27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17141187 17141187] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Chi, S | + | [[Category: Chi, S W.]] |
| - | [[Category: Han, K | + | [[Category: Han, K H.]] |
[[Category: amphipathic helix]] | [[Category: amphipathic helix]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:29:34 2008'' |
Revision as of 15:29, 21 February 2008
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The High-resolution Solution Conformation of an Antimicrobial Peptide Gaegurin 4 and Its Mode of Membrane Interaction
Overview
We have applied NMR spectroscopy to determine the high-resolution structure of gaegurin 4, a 37-residue antimicrobial peptide from Rana rugosa, under varying hydrophobic conditions. Even in 100% H2O, gaegurin 4 contains a nascent turn near its C-terminal Rana box. Under a more hydrophobic condition it forms two amphipathic helices, one long encompassing residues 2-23 and the other consisting of residues 25-34, similar to what has been observed in cecropin A. Functional implication of the helix-breaking kink at Gly24 in gaegurin 4 was investigated by preparing several analogs. Based upon the current and previous results, we propose a novel seaanemone-like ion pore-forming model for gaegurin 4.
About this Structure
2G9L is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Solution structure and membrane interaction mode of an antimicrobial peptide gaegurin 4., Chi SW, Kim JS, Kim DH, Lee SH, Park YH, Han KH, Biochem Biophys Res Commun. 2007 Jan 19;352(3):592-7. Epub 2006 Nov 27. PMID:17141187
Page seeded by OCA on Thu Feb 21 17:29:34 2008
