1lfc

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[[Image:1lfc.png|left|200px]]
 
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{{STRUCTURE_1lfc| PDB=1lfc | SCENE= }}
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==BOVINE LACTOFERRICIN (LFCINB), NMR, 20 STRUCTURES==
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<StructureSection load='1lfc' size='340' side='right'caption='[[1lfc]]' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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</table>
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== Function ==
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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===BOVINE LACTOFERRICIN (LFCINB), NMR, 20 STRUCTURES===
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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>
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{{ABSTRACT_PUBMED_9521752}}
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==About this Structure==
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<div class="pdbe-citations 1lfc" style="background-color:#fffaf0;"></div>
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[[1lfc]] is a 1 chain structure of [[Lactoferrin]] and [[Transferrin]] with 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].
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==See Also==
==See Also==
*[[Lactoferrin|Lactoferrin]]
*[[Lactoferrin|Lactoferrin]]
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*[[Transferrin|Transferrin]]
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*[[Transferrin 3D structures|Transferrin 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:009521752</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Arrowsmith, C H.]]
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[[Category: Large Structures]]
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[[Category: Hwang, P M.]]
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[[Category: Arrowsmith CH]]
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[[Category: Shan, X.]]
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[[Category: Hwang PM]]
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[[Category: Vogel, H J.]]
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[[Category: Shan X]]
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[[Category: Zhou, N.]]
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[[Category: Vogel HJ]]
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[[Category: Antimicrobial peptide]]
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[[Category: Zhou N]]
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[[Category: Iron transport]]
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[[Category: Proteolytic fragment]]
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Current revision

BOVINE LACTOFERRICIN (LFCINB), NMR, 20 STRUCTURES

PDB ID 1lfc

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