1lfc
From Proteopedia
(New page: 200px<br /><applet load="1lfc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lfc" /> '''BOVINE LACTOFERRICIN (LFCINB), NMR, 20 STRUC...) |
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| - | [[Image:1lfc.gif|left|200px]]<br /><applet load="1lfc" size=" | + | [[Image:1lfc.gif|left|200px]]<br /><applet load="1lfc" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''BOVINE LACTOFERRICIN (LFCINB), NMR, 20 STRUCTURES'''<br /> | '''BOVINE LACTOFERRICIN (LFCINB), NMR, 20 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The solution structure of bovine lactoferricin (LfcinB) has been | + | The solution structure of bovine lactoferricin (LfcinB) has been determined using 2D 1H NMR spectroscopy. LfcinB is a 25-residue antimicrobial peptide released by pepsin cleavage of lactoferrin, an 80 kDa iron-binding glycoprotein with many immunologically important functions. The NMR structure of LfcinB reveals a somewhat distorted antiparallel beta-sheet. This contrasts with the X-ray structure of bovine lactoferrin, in which residues 1-13 (of LfcinB) form an alpha-helix. Hence, this region of lactoferricin B appears able to adopt a helical or sheetlike conformation, similar to what has been proposed for the amyloidogenic prion proteins and Alzheimer's beta-peptides. LfcinB has an extended hydrophobic surface comprised of residues Phe1, Cys3, Trp6, Trp8, Pro16, Ile18, and Cys20. The side chains of these residues are well-defined in the NMR structure. Many hydrophilic and positively charged residues surround the hydrophobic surface, giving LfcinB an amphipathic character. LfcinB bears numerous similarities to a vast number of cationic peptides which exert their antimicrobial activities through membrane disruption. The structures of many of these peptides have been well characterized, and models of their membrane-permeabilizing mechanisms have been proposed. The NMR solution structure of LfcinB may be more relevant to membrane interaction than that suggested by the X-ray structure of intact lactoferrin. Based on the solution structure, it is now possible to propose potential mechanisms for the antimicrobial action of LfcinB. |
==About this Structure== | ==About this Structure== | ||
| - | 1LFC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http:// | + | 1LFC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LFC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Arrowsmith, C | + | [[Category: Arrowsmith, C H.]] |
| - | [[Category: Hwang, P | + | [[Category: Hwang, P M.]] |
[[Category: Shan, X.]] | [[Category: Shan, X.]] | ||
| - | [[Category: Vogel, H | + | [[Category: Vogel, H J.]] |
[[Category: Zhou, N.]] | [[Category: Zhou, N.]] | ||
[[Category: antimicrobial peptide]] | [[Category: antimicrobial peptide]] | ||
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[[Category: proteolytic fragment]] | [[Category: proteolytic fragment]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:44:29 2008'' |
Revision as of 11:44, 21 February 2008
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BOVINE LACTOFERRICIN (LFCINB), NMR, 20 STRUCTURES
Overview
The solution structure of bovine lactoferricin (LfcinB) has been determined using 2D 1H NMR spectroscopy. LfcinB is a 25-residue antimicrobial peptide released by pepsin cleavage of lactoferrin, an 80 kDa iron-binding glycoprotein with many immunologically important functions. The NMR structure of LfcinB reveals a somewhat distorted antiparallel beta-sheet. This contrasts with the X-ray structure of bovine lactoferrin, in which residues 1-13 (of LfcinB) form an alpha-helix. Hence, this region of lactoferricin B appears able to adopt a helical or sheetlike conformation, similar to what has been proposed for the amyloidogenic prion proteins and Alzheimer's beta-peptides. LfcinB has an extended hydrophobic surface comprised of residues Phe1, Cys3, Trp6, Trp8, Pro16, Ile18, and Cys20. The side chains of these residues are well-defined in the NMR structure. Many hydrophilic and positively charged residues surround the hydrophobic surface, giving LfcinB an amphipathic character. LfcinB bears numerous similarities to a vast number of cationic peptides which exert their antimicrobial activities through membrane disruption. The structures of many of these peptides have been well characterized, and models of their membrane-permeabilizing mechanisms have been proposed. The NMR solution structure of LfcinB may be more relevant to membrane interaction than that suggested by the X-ray structure of intact lactoferrin. Based on the solution structure, it is now possible to propose potential mechanisms for the antimicrobial action of LfcinB.
About this Structure
1LFC is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin., Hwang PM, Zhou N, Shan X, Arrowsmith CH, Vogel HJ, Biochemistry. 1998 Mar 24;37(12):4288-98. PMID:9521752
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