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Crystal Structure of Hemolin: A Horseshoe Shape with Implications for Homophilic Adhesion

Science  14 Aug 1998:
Vol. 281, Issue 5379, pp. 991-995
DOI: 10.1126/science.281.5379.991

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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.

  • * Present address: Department of Molecular Biophysics, Center for Chemistry and Chemical Engineering, Post Office Box 124, Lund University, S-221 00 Lund, Sweden.

  • Present address: AFMB, CNRS UPR 9039, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France.

  • Present address: Cold Spring Harbor Laboratory, 1 Bungtown Road, Cold Spring Harbor, NY 11724, USA.

  • § To whom correspondence should be addressed. E-mail: bjorkman{at}cco.caltech.edu

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