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Article

The crystal structure of lipopolysaccharide binding protein reveals the location of a frequent mutation that impairs innate immunity.

Immunity - 17 Oct 2013

Eckert Jana K, Kim Young J, Kim Jung I, Gürtler Kathleen, Oh Djin-Ye, Sur Saubashya, Lundvall Linn, Hamann Lutz, van der Ploeg Anke, Pickkers Peter, Giamarellos-Bourboulis Evangelos, Kubarenko Andriy V, Weber Alexander N, Kabesch Michael, Kumpf Oliver, An Hyun-Jung, Lee Jie-Oh, Schumann Ralf R

Abstract excerpt

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...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 24120359
DOI: 10.1016/j.immuni.2013.09.005

Genes

LBP
BPI

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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