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Science 14 August 1998:
Vol. 281. no. 5379, pp. 991 - 995
DOI: 10.1126/science.281.5379.991
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Reports

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

Xiao-Dong Su, * Louis N. Gastinel, dagger Daniel E. Vaughn, ddagger Ingrid Faye, Pak Poon, Pamela J. Bjorkman §

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.

X.-D. Su, L. N. Gastinel, P. J. Bjorkman, Division of Biology 156-29 and Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA. D. E. Vaughn, Division of Biology 156-29, California Institute of Technology, Pasadena, CA 91125, USA. I. Faye, Department of Genetics, Stockholm University, S-106 91 Stockholm, Sweden. P. Poon, Department of Chemistry and Biochemistry, University of California at Los Angeles, Los Angeles, CA 90095, USA.
*   Present address: Department of Molecular Biophysics, Center for Chemistry and Chemical Engineering, Post Office Box 124, Lund University, S-221 00 Lund, Sweden.

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

ddagger    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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