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New page: left|200px<br /><applet load="1lyp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lyp" /> '''THE SOLUTION STRUCTURE OF THE ACTIVE DOMAIN ... |
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== | ==THE SOLUTION STRUCTURE OF THE ACTIVE DOMAIN OF CAP18: A LIPOPOLYSACCHARIDE BINDING PROTEIN FROM RABBIT LEUKOCYTES== | ||
We have employed the circular dichroism (CD) technique to characterize the | <StructureSection load='1lyp' size='340' side='right'caption='[[1lyp]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1lyp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LYP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LYP 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=1lyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lyp OCA], [https://pdbe.org/1lyp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lyp RCSB], [https://www.ebi.ac.uk/pdbsum/1lyp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lyp ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CAP18_RABIT CAP18_RABIT] CAP18 binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria. Has antibiotic activity. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We have employed the circular dichroism (CD) technique to characterize the solution structure of CAP18(106-137), a lipopolysaccharide (LPS) binding, antimicrobial protein, and its interaction with lipid A. Our results revealed that CAP18(106-137) may exist in at least three lipid A concentration-dependent, primarily helix conformations. The 'model' structure of CAP18(106-137) in 30% (v/v) TFE, determined by nuclear magnetic resonance (NMR) technique, was found to be a complete and very rigid helix. In this conformation, the cationic and hydrophobic groups of CAP18(106-137) are separated into patches and stripes in such a way that it can favorably interact with lipid A through either coulombic interaction with the diphosphoryl groups or hydrophobic interaction with the fatty acyl chains. | |||
The solution structure of the active domain of CAP18--a lipopolysaccharide binding protein from rabbit leukocytes.,Chen C, Brock R, Luh F, Chou PJ, Larrick JW, Huang RF, Huang TH FEBS Lett. 1995 Aug 14;370(1-2):46-52. PMID:7649303<ref>PMID:7649303</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1lyp" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Chen C]] | |||
[[Category: Chen | [[Category: Huang T-H]] | ||
[[Category: Huang | |||
Latest revision as of 21:48, 29 November 2023
THE SOLUTION STRUCTURE OF THE ACTIVE DOMAIN OF CAP18: A LIPOPOLYSACCHARIDE BINDING PROTEIN FROM RABBIT LEUKOCYTESTHE SOLUTION STRUCTURE OF THE ACTIVE DOMAIN OF CAP18: A LIPOPOLYSACCHARIDE BINDING PROTEIN FROM RABBIT LEUKOCYTES
Structural highlights
FunctionCAP18_RABIT CAP18 binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria. Has antibiotic activity. Publication Abstract from PubMedWe have employed the circular dichroism (CD) technique to characterize the solution structure of CAP18(106-137), a lipopolysaccharide (LPS) binding, antimicrobial protein, and its interaction with lipid A. Our results revealed that CAP18(106-137) may exist in at least three lipid A concentration-dependent, primarily helix conformations. The 'model' structure of CAP18(106-137) in 30% (v/v) TFE, determined by nuclear magnetic resonance (NMR) technique, was found to be a complete and very rigid helix. In this conformation, the cationic and hydrophobic groups of CAP18(106-137) are separated into patches and stripes in such a way that it can favorably interact with lipid A through either coulombic interaction with the diphosphoryl groups or hydrophobic interaction with the fatty acyl chains. The solution structure of the active domain of CAP18--a lipopolysaccharide binding protein from rabbit leukocytes.,Chen C, Brock R, Luh F, Chou PJ, Larrick JW, Huang RF, Huang TH FEBS Lett. 1995 Aug 14;370(1-2):46-52. PMID:7649303[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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