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4M4D

Crystal structure of lipopolysaccharide binding protein

Summary for 4M4D
Entry DOI10.2210/pdb4m4d/pdb
DescriptorLipopolysaccharide-binding protein, 2-acetamido-2-deoxy-beta-D-glucopyranose, 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE (3 entities in total)
Functional Keywordsbeta barrel, immune response, lipopolysaccharide, blood, lipid binding protein
Biological sourceMus musculus (mouse)
Total number of polymer chains2
Total formula weight107405.58
Authors
Primary citationEckert, J.K.,Kim, Y.J.,Kim, J.I.,Gurtler, K.,Oh, D.Y.,Sur, S.,Lundvall, L.,Hamann, L.,van der Ploeg, A.,Pickkers, P.,Giamarellos-Bourboulis, E.,Kubarenko, A.V.,Weber, A.N.,Kabesch, M.,Kumpf, O.,An, H.J.,Lee, J.O.,Schumann, R.R.
The crystal structure of lipopolysaccharide binding protein reveals the location of a frequent mutation that impairs innate immunity.
Immunity, 39:647-660, 2013
Cited by
PubMed Abstract: Lipopolysaccharide (LPS) binding protein (LBP) is an acute-phase protein that initiates an immune response after recognition of bacterial LPS. Here, we report the crystal structure of murine LBP at 2.9 Å resolution. Several structural differences were observed between LBP and the related bactericidal/permeability-increasing protein (BPI), and the LBP C-terminal domain contained a negatively charged groove and a hydrophobic "phenylalanine core." A frequent human LBP SNP (allelic frequency 0.08) affected this region, potentially generating a proteinase cleavage site. The mutant protein had a reduced binding capacity for LPS and lipopeptides. SNP carriers displayed a reduced cytokine response after in vivo LPS exposure and lower cytokine concentrations in pneumonia. In a retrospective trial, the LBP SNP was associated with increased mortality rates during sepsis and pneumonia. Thus, the structural integrity of LBP may be crucial for fighting infections efficiently, and future patient stratification might help to develop better therapeutic strategies.
PubMed: 24120359
DOI: 10.1016/j.immuni.2013.09.005
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.909 Å)
Structure validation

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