1lfc: Difference between revisions
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New page: left|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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== | ==BOVINE LACTOFERRICIN (LFCINB), NMR, 20 STRUCTURES== | ||
The solution structure of bovine lactoferricin (LfcinB) has been | <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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1lfc" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Lactoferrin|Lactoferrin]] | |||
*[[Transferrin 3D structures|Transferrin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Arrowsmith | [[Category: Arrowsmith CH]] | ||
[[Category: Hwang | [[Category: Hwang PM]] | ||
[[Category: Shan | [[Category: Shan X]] | ||
[[Category: Vogel | [[Category: Vogel HJ]] | ||
[[Category: Zhou | [[Category: Zhou N]] | ||
