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Updated: Aug 16, 2026

High-throughput Crystallization of Membrane Proteins Using the Lipidic Bicelle Method
Published on: January 9, 2012
Crystal structure of hemolin: a horseshoe shape with implications for homophilic adhesion
X D Su1, L N Gastinel, D E Vaughn
1Division of Biology 156-29 and Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA.
Abstract:
Hemolin, an insect immunoglobulin superfamily member, is a lipopolysaccharide-binding immune protein induced during bacterial infection. The 3.1 angstrom crystal structure reveals a bound phosphate and patches of positive charge, which may represent the lipopolysaccharide binding site, and a new and unexpected arrangement of four immunoglobulin-like domains forming a horseshoe. Sequence analysis and analytical ultracentrifugation suggest that the domain arrangement is a feature of the L1 family of neural cell adhesion molecules related to hemolin. These results are relevant to interpretation of human L1 mutations in neurological diseases and suggest a domain swapping model for how L1 family proteins mediate homophilic adhesion.
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