1lfc
From Proteopedia
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| - | [[Image:1lfc.gif|left|200px]] | + | [[Image:1lfc.gif|left|200px]] |
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| - | '''BOVINE LACTOFERRICIN (LFCINB), NMR, 20 STRUCTURES''' | + | {{Structure |
| + | |PDB= 1lfc |SIZE=350|CAPTION= <scene name='initialview01'>1lfc</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''BOVINE LACTOFERRICIN (LFCINB), NMR, 20 STRUCTURES''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LFC is a [ | + | 1LFC is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9521752 9521752] |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: proteolytic fragment]] | [[Category: proteolytic fragment]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:30:18 2008'' |
Revision as of 10:30, 20 March 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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