1lyp
THE SOLUTION STRUCTURE OF THE ACTIVE DOMAIN OF CAP18: A LIPOPOLYSACCHARIDE BINDING PROTEIN FROM RABBIT LEUKOCYTES
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
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.
About this StructureAbout this Structure
1LYP is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.
ReferenceReference
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
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