1xv4: Difference between revisions

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-{{Seed}}
-[[Image:1xv4.png|left|200px]]
-<!--
+==Solution structure of antimicrobial and endotoxin-neutralizing peptide Lf11 in SDS micelles==
-The line below this paragraph, containing "STRUCTURE_1xv4", creates the "Structure Box" on the page.
+<StructureSection load='1xv4' size='340' side='right'caption='[[1xv4]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1xv4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XV4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XV4 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 7 models</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>
-{{STRUCTURE_1xv4|  PDB=1xv4  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xv4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xv4 OCA], [https://pdbe.org/1xv4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xv4 RCSB], [https://www.ebi.ac.uk/pdbsum/1xv4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xv4 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TRFL_HUMAN TRFL_HUMAN] 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:12535064</ref> <ref>PMID:22320386</ref>   Lactotransferrin has antimicrobial activity which depends on the extracellular cation concentration.<ref>PMID:12535064</ref> <ref>PMID:22320386</ref>   Lactoferroxins A, B and C have opioid antagonist activity. Lactoferroxin A shows preference for mu-receptors, while lactoferroxin B and C have somewhat higher degrees of preference for kappa-receptors than for mu-receptors.<ref>PMID:12535064</ref> <ref>PMID:22320386</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:12535064</ref> <ref>PMID:22320386</ref>   Isoform DeltaLf: transcription factor with antiproliferative properties and inducing cell cycle arrest. Binds to DeltaLf response element found in the SKP1, BAX, DCPS, and SELH promoters.<ref>PMID:12535064</ref> <ref>PMID:22320386</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Treatment of Gram-negative bacterial infections with antimicrobial agents can cause release of the endotoxin lipopolysaccharide (LPS), the potent initiator of sepsis, which is the major cause of mortality in intensive care units worldwide. Structural information on peptides bound to LPS can lead to the development of more effective endotoxin neutralizers. Short linear antimicrobial and endotoxin-neutralizing peptide LF11, based on the human lactoferrin, binds to LPS, inducing a peptide fold with a "T-shaped" arrangement of a hydrophobic core and two clusters of basic residues that match the distance between the two phosphate groups of LPS. Side chain arrangement of LF11 bound to LPS extends the previously proposed LPS binding pattern, emphasizing the importance of both electrostatic and hydrophobic interactions in a defined geometric arrangement. In anionic micelles, the LF11 forms amphipathic conformation with a smaller hydrophobic core than in LPS, whereas in zwitterionic micelles, the structure is even less defined. Protection of tryptophan fluorescence quenching in the order SDS&gt;LPS&gt;DPC and hydrogen exchange protection indicates the decreasing extent of insertion of the N terminus and potential role of peptide plasticity in differentiation between bacterial and eukaryotic membranes.
-===Solution structure of antimicrobial and endotoxin-neutralizing peptide Lf11 in SDS micelles===
+Structural origin of endotoxin neutralization and antimicrobial activity of a lactoferrin-based peptide.,Japelj B, Pristovsek P, Majerle A, Jerala R J Biol Chem. 2005 Apr 29;280(17):16955-61. Epub 2005 Feb 1. PMID:15687491<ref>PMID:15687491</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1xv4" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_15687491}}, adds the Publication Abstract to the page
+*[[Lactoferrin|Lactoferrin]]
-(as it appears on PubMed at http://www.pubmed.gov), where 15687491 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_15687491}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Homo sapiens]]
-Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XV4 OCA].
+[[Category: Large Structures]]
+[[Category: Japelj B]]
-==Reference==
+[[Category: Jerala R]]
-Structural origin of endotoxin neutralization and antimicrobial activity of a lactoferrin-based peptide., Japelj B, Pristovsek P, Majerle A, Jerala R, J Biol Chem. 2005 Apr 29;280(17):16955-61. Epub 2005 Feb 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15687491 15687491]
+[[Category: Majerle A]]
-[[Category: Japelj, B.]]
+[[Category: Pristovsek P]]
-[[Category: Jerala, R.]]
-[[Category: Majerle, A.]]
-[[Category: Pristovsek, P.]]
-[[Category: Hydrophobic core]]
-[[Category: Loop]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:58:16 2008''