Backbone and side chain chemical shift assignments of apolipophorin III from Galleria mellonella

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• 作者：Karin A. Crowhurst ; James V.C. Horn ; Paul M.M. Weers
• 关键词：Apolipophorin III ; Exchangeable apolipoprotein ; apoLp ; III ; Galleria mellonella ; NMR ; Chemical shift assignment
• 刊名：Biomolecular NMR Assignments
• 出版年：2016
• 出版时间：April 2016
• 年：2016
• 卷：10
• 期：1
• 页码：143-147
• 全文大小：570 KB
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• 作者单位：Karin A. Crowhurst (1)
  James V.C. Horn (2)
  Paul M.M. Weers (2)
  
  1. Department of Chemistry and Biochemistry, California State University Northridge, 18111 Nordhoff St., Northridge, CA, 91330-8262, USA
  2. Department of Chemistry and Biochemistry, California State University Long Beach, 1250 Bellflower Blvd., Long Beach, CA, 90840-9507, USA
  
• 刊物类别：Physics and Astronomy
• 刊物主题：None Assigned
• 出版者：Springer Netherlands
• ISSN：1874-270X

文摘

Apolipophorin III, a 163 residue monomeric protein from the greater wax moth Galleria mellonella (abbreviated as apoLp-III_GM), has roles in upregulating expression of antimicrobial proteins as well as binding and deforming bacterial membranes. Due to its similarity to vertebrate apolipoproteins there is interest in performing atomic resolution analysis of apoLp-III_GM as part of an effort to better understand its mechanism of action in innate immunity. In the first step towards structural characterization of apoLp-III_GM, 99 % of backbone and 88 % of side chain 1H, 13C and 15N chemical shifts were assigned. TALOS+ analysis of the backbone resonances has predicted that the protein is composed of five long helices, which is consistent with the reported structures of apolipophorins from other insect species. The next stage in the characterization of apoLp-III from G. mellonella will be to utilize these resonance assignments in solving the solution structure of this protein.