Download MendeleyCrystal structure of hemolin: a horseshoe shape with implications for homophilic adhesion.
Su, X.D., Gastinel, L.N., Vaughn, D.E., Faye, I., Poon, P., Bjorkman, P.J.(1998) Science 281: 991-995
- PubMed: 9703515
- DOI: https://doi.org/10.1126/science.281.5379.991
- Primary Citation of Related Structures:
1BIH - PubMed 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.
Organizational Affiliation:
Division of Biology 156-29 and Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA.
