Published August 14, 1998
| public
Journal Article
Crystal Structure of Hemolin: A Horseshoe Shape with Implications for Homophilic Adhesion
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.
Additional Information
© 1998 American Association for the Advancement of Science. Received 20 April 1998; accepted 1 July 1998. We thank T. O. Yeates for help with the Dom_angle program, H. P. Erickson for valuable discussions about ultracentrifugation data, A. J. Bieber for communicating results before publication, the Caltech PPMAL for mass spectrometry analyses, P. M. Snow and I. Nangiana for help with protein expression, Q. R. Fan for the KIR coordinates, and M. J. Bennett, L. M. Sánchez, and A. J. Chirino for discussions and help with crystallographic software. Hemolin coordinates have been deposited in the PDB (1BIH).Additional details
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