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1y58

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The structure of a lactoferricinB derivative bound to micelles

Structural highlights

1y58 is a 1 chain structure with sequence from Bos taurus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2] Lactotransferrin has antimicrobial activity. The most effective inhibitory activity was seen against E.coli and P.aeruginosa.^[3] ^[4] Lactoferricin B is an antimicrobial peptide. Inhibits the growth of Gram-negative and Gram-positive bacteria.^[5] ^[6] 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.^[7] ^[8]

Publication Abstract from PubMed

The powerful antimicrobial properties of bovine lactoferricin (LfcinB) make it attractive for the development of new antimicrobial agents. An 11-residue linear peptide portion of LfcinB has been reported to have similar antimicrobial activity to lactoferricin itself, but with lower hemolytic activity. The membrane-binding and membrane-perturbing properties of this peptide were studied together with an amidated synthetic version with an added disulfide bond, which was designed to confer increased stability and possibly activity. The antimicrobial and cytotoxic properties of the peptides were measured against Staphylococcus aureus and Escherichia coli and by hemolysis assays. The peptides were also tested in an anti-cancer assay against neuroblastoma cell lines. Vesicle disruption caused by these LfcinB derivatives was studied using the fluorescent reporter molecule calcein. The extent of burial of the two Trp residues in membrane mimetic environments were quantitated by fluorescence. Finally, the solution NMR structures of the peptides bound to SDS micelles were determined to provide insight into their membrane bound state. The cyclic peptide was found to have greater antimicrobial potency than its linear counterpart. Consistent with this property, the two Trp residues of the modified peptide were suggested to be embedded deeper into the membrane. Although both peptides adopt an amphipathic structure without any regular alpha-helical or beta-sheet conformation, the 3D-structures revealed a clearer partitioning of the cationic and hydrophobic faces for the cyclic peptide.

Structural studies and model membrane interactions of two peptides derived from bovine lactoferricin.,Nguyen LT, Schibli DJ, Vogel HJ J Pept Sci. 2005 Jul;11(7):379-89. PMID:15635665^[9]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hoek KS, Milne JM, Grieve PA, Dionysius DA, Smith R. Antibacterial activity in bovine lactoferrin-derived peptides. Antimicrob Agents Chemother. 1997 Jan;41(1):54-9. PMID:8980754
↑ Massucci MT, Giansanti F, Di Nino G, Turacchio M, Giardi MF, Botti D, Ippoliti R, De Giulio B, Siciliano RA, Donnarumma G, Valenti P, Bocedi A, Polticelli F, Ascenzi P, Antonini G. Proteolytic activity of bovine lactoferrin. Biometals. 2004 Jun;17(3):249-55. PMID:15222473
↑ Hoek KS, Milne JM, Grieve PA, Dionysius DA, Smith R. Antibacterial activity in bovine lactoferrin-derived peptides. Antimicrob Agents Chemother. 1997 Jan;41(1):54-9. PMID:8980754
↑ Massucci MT, Giansanti F, Di Nino G, Turacchio M, Giardi MF, Botti D, Ippoliti R, De Giulio B, Siciliano RA, Donnarumma G, Valenti P, Bocedi A, Polticelli F, Ascenzi P, Antonini G. Proteolytic activity of bovine lactoferrin. Biometals. 2004 Jun;17(3):249-55. PMID:15222473
↑ Hoek KS, Milne JM, Grieve PA, Dionysius DA, Smith R. Antibacterial activity in bovine lactoferrin-derived peptides. Antimicrob Agents Chemother. 1997 Jan;41(1):54-9. PMID:8980754
↑ Massucci MT, Giansanti F, Di Nino G, Turacchio M, Giardi MF, Botti D, Ippoliti R, De Giulio B, Siciliano RA, Donnarumma G, Valenti P, Bocedi A, Polticelli F, Ascenzi P, Antonini G. Proteolytic activity of bovine lactoferrin. Biometals. 2004 Jun;17(3):249-55. PMID:15222473
↑ Hoek KS, Milne JM, Grieve PA, Dionysius DA, Smith R. Antibacterial activity in bovine lactoferrin-derived peptides. Antimicrob Agents Chemother. 1997 Jan;41(1):54-9. PMID:8980754
↑ Massucci MT, Giansanti F, Di Nino G, Turacchio M, Giardi MF, Botti D, Ippoliti R, De Giulio B, Siciliano RA, Donnarumma G, Valenti P, Bocedi A, Polticelli F, Ascenzi P, Antonini G. Proteolytic activity of bovine lactoferrin. Biometals. 2004 Jun;17(3):249-55. PMID:15222473
↑ Nguyen LT, Schibli DJ, Vogel HJ. Structural studies and model membrane interactions of two peptides derived from bovine lactoferricin. J Pept Sci. 2005 Jul;11(7):379-89. PMID:15635665 doi:10.1002/psc.629

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1y58"

Categories: Bos taurus | Large Structures | Nguyen LT | Schibli DJ | Vogel HJ

@@ Line 1: / Line 1: @@
 ==The structure of a lactoferricinB derivative bound to micelles==
-<StructureSection load='1y58' size='340' side='right' caption='[[1y58]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='1y58' size='340' side='right'caption='[[1y58]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1y58]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y58 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Y58 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1y58]] 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=1Y58 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y58 FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1lfc|1lfc]], [[1y5c|1y5c]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y58 OCA], [http://pdbe.org/1y58 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y58 RCSB], [http://www.ebi.ac.uk/pdbsum/1y58 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1y58 ProSAT]</span></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=1y58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y58 OCA], [https://pdbe.org/1y58 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y58 RCSB], [https://www.ebi.ac.uk/pdbsum/1y58 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y58 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 ==
@@ Line 17: / Line 19: @@
 </div>
 <div class="pdbe-citations 1y58" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Lactoferrin|Lactoferrin]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Nguyen, L T]]
+[[Category: Bos taurus]]
-[[Category: Schibli, D J]]
+[[Category: Large Structures]]
-[[Category: Vogel, H J]]
+[[Category: Nguyen LT]]
-[[Category: Amidated c-terminus]]
+[[Category: Schibli DJ]]
-[[Category: Disulfide-linked]]
+[[Category: Vogel HJ]]
-[[Category: Micelle-bound]]
-[[Category: Transport protein]]

1y58

From Proteopedia

Current revision

The structure of a lactoferricinB derivative bound to micelles

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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