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1lfc

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[[Image:1lfc.gif|left|200px]]
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{{STRUCTURE_1lfc| PDB=1lfc | SCENE= }}
{{STRUCTURE_1lfc| PDB=1lfc | SCENE= }}
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'''BOVINE LACTOFERRICIN (LFCINB), NMR, 20 STRUCTURES'''
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===BOVINE LACTOFERRICIN (LFCINB), NMR, 20 STRUCTURES===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 9521752 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9521752}}
==About this Structure==
==About this Structure==
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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].
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1LFC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LFC OCA].
==Reference==
==Reference==
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[[Category: Iron transport]]
[[Category: Iron transport]]
[[Category: Proteolytic fragment]]
[[Category: Proteolytic fragment]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:52:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 19:07:58 2008''

Revision as of 16:15, 2 July 2008

Image:1lfc.png

Template:STRUCTURE 1lfc

BOVINE LACTOFERRICIN (LFCINB), NMR, 20 STRUCTURES

Template:ABSTRACT PUBMED 9521752

About this Structure

1LFC is a Single protein structure of sequence from Bos taurus. Full experimental 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

Page seeded by OCA on Wed Jul 2 19:07:58 2008

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