2amn: Difference between revisions

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-[[Image:2amn.gif|left|200px]]<br /><applet load="2amn" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="2amn" />
-'''Solution structure of Fowlicidin-1, a novel Cathelicidin antimicrobial peptide from chicken'''<br />
-==Overview==
+==Solution structure of Fowlicidin-1, a novel Cathelicidin antimicrobial peptide from chicken==
-Cationic antimicrobial peptides are naturally occurring antibiotics that, are actively being explored as a new class of anti-infective agents. We, recently identified three cathelicidin antimicrobial peptides from, chicken, which have potent and broad-spectrum antibacterial activities in, vitro (Xiao Y, Cai Y, Bommineni YR, Fernando SC, Prakash O, Gilliland SE &amp;, Zhang G (2006) J Biol Chem281, 2858-2867). Here we report that, fowlicidin-1 mainly adopts an alpha-helical conformation with a slight, kink induced by glycine close to the center, in addition to a short, flexible unstructured region near the N terminus. To gain further insight, into the structural requirements for function, a series of truncation and, substitution mutants of fowlicidin-1 were synthesized and tested, separately for their antibacterial, cytolytic and lipopolysaccharide, (LPS)-binding activities. The short C-terminal helical segment after the, kink, consisting of a stretch of eight amino acids (residues 16-23), was, shown to be critically involved in all three functions, suggesting that, this region may be required for the peptide to interact with LPS and lipid, membranes and to permeabilize both prokaryotic and eukaryotic cells. We, also identified a second segment, comprising three amino acids (residues, 5-7) in the N-terminal flexible region, that participates in LPS binding, and cytotoxicity but is less important in bacterial killing. The, fowlicidin-1 analog, with deletion of the second N-terminal segment, (residues 5-7), was found to retain substantial antibacterial potency with, a significant reduction in cytotoxicity. Such a peptide analog may have, considerable potential for development as an anti-infective agent.
+<StructureSection load='2amn' size='340' side='right'caption='[[2amn]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2amn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AMN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AMN FirstGlance]. <br>
+</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2amn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2amn OCA], [https://pdbe.org/2amn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2amn RCSB], [https://www.ebi.ac.uk/pdbsum/2amn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2amn ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CTHL1_CHICK CTHL1_CHICK] Binds bacterial lipopolysaccharide (LPS). Has potent antimicrobial activity against Gram-positive and Gram-negative bacteria (in vitro). Has hemolytic activity (in vitro). May play a role in the innate immune response.<ref>PMID:16326712</ref> <ref>PMID:16817888</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Cationic antimicrobial peptides are naturally occurring antibiotics that are actively being explored as a new class of anti-infective agents. We recently identified three cathelicidin antimicrobial peptides from chicken, which have potent and broad-spectrum antibacterial activities in vitro (Xiao Y, Cai Y, Bommineni YR, Fernando SC, Prakash O, Gilliland SE &amp; Zhang G (2006) J Biol Chem281, 2858-2867). Here we report that fowlicidin-1 mainly adopts an alpha-helical conformation with a slight kink induced by glycine close to the center, in addition to a short flexible unstructured region near the N terminus. To gain further insight into the structural requirements for function, a series of truncation and substitution mutants of fowlicidin-1 were synthesized and tested separately for their antibacterial, cytolytic and lipopolysaccharide (LPS)-binding activities. The short C-terminal helical segment after the kink, consisting of a stretch of eight amino acids (residues 16-23), was shown to be critically involved in all three functions, suggesting that this region may be required for the peptide to interact with LPS and lipid membranes and to permeabilize both prokaryotic and eukaryotic cells. We also identified a second segment, comprising three amino acids (residues 5-7) in the N-terminal flexible region, that participates in LPS binding and cytotoxicity but is less important in bacterial killing. The fowlicidin-1 analog, with deletion of the second N-terminal segment (residues 5-7), was found to retain substantial antibacterial potency with a significant reduction in cytotoxicity. Such a peptide analog may have considerable potential for development as an anti-infective agent.
-==About this Structure==
+Structure-activity relationships of fowlicidin-1, a cathelicidin antimicrobial peptide in chicken.,Xiao Y, Dai H, Bommineni YR, Soulages JL, Gong YX, Prakash O, Zhang G FEBS J. 2006 Jun;273(12):2581-93. PMID:16817888<ref>PMID:16817888</ref>
-AMN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AMN OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Structure-activity relationships of fowlicidin-1, a cathelicidin antimicrobial peptide in chicken., Xiao Y, Dai H, Bommineni YR, Soulages JL, Gong YX, Prakash O, Zhang G, FEBS J. 2006 Jun;273(12):2581-93. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16817888 16817888]
+</div>
-[[Category: Single protein]]
+<div class="pdbe-citations 2amn" style="background-color:#fffaf0;"></div>
-[[Category: Bommineni, Y.R.]]
+== References ==
-[[Category: Dai, H.]]
+<references/>
-[[Category: Prakash, O.]]
+__TOC__
-[[Category: Xiao, Y.]]
+</StructureSection>
-[[Category: Zhang, G.]]
+[[Category: Gallus gallus]]
-[[Category: linear helix]]
+[[Category: Large Structures]]
+[[Category: Bommineni YR]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 18:05:33 2008''
+[[Category: Dai H]]
+[[Category: Prakash O]]
+[[Category: Xiao Y]]
+[[Category: Zhang G]]