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[[Image:1lfc.gif|left|200px]]
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{{STRUCTURE_1lfc|  PDB=1lfc  |  SCENE=  }}
'''BOVINE LACTOFERRICIN (LFCINB), NMR, 20 STRUCTURES'''


==BOVINE LACTOFERRICIN (LFCINB), NMR, 20 STRUCTURES==
<StructureSection load='1lfc' size='340' side='right'caption='[[1lfc]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1lfc]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LFC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lfc OCA], [https://pdbe.org/1lfc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lfc RCSB], [https://www.ebi.ac.uk/pdbsum/1lfc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lfc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TRFL_BOVIN TRFL_BOVIN] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate.<ref>PMID:8980754</ref> <ref>PMID:15222473</ref>  Lactotransferrin has antimicrobial activity. The most effective inhibitory activity was seen against E.coli and P.aeruginosa.<ref>PMID:8980754</ref> <ref>PMID:15222473</ref>  Lactoferricin B is an antimicrobial peptide. Inhibits the growth of Gram-negative and Gram-positive bacteria.<ref>PMID:8980754</ref> <ref>PMID:15222473</ref>  The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity.<ref>PMID:8980754</ref> <ref>PMID:15222473</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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<ref>PMID:9521752</ref>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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].
</div>
<div class="pdbe-citations 1lfc" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[Lactoferrin|Lactoferrin]]
*[[Transferrin 3D structures|Transferrin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C H.]]
[[Category: Arrowsmith CH]]
[[Category: Hwang, P M.]]
[[Category: Hwang PM]]
[[Category: Shan, X.]]
[[Category: Shan X]]
[[Category: Vogel, H J.]]
[[Category: Vogel HJ]]
[[Category: Zhou, N.]]
[[Category: Zhou N]]
[[Category: Antimicrobial peptide]]
[[Category: Iron transport]]
[[Category: Proteolytic fragment]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 23:52:16 2008''
Retrieved from "https://proteopedia.org/1lfc"