1BIH

CRYSTAL STRUCTURE OF THE INSECT IMMUNE PROTEIN HEMOLIN: A NEW DOMAIN ARRANGEMENT WITH IMPLICATIONS FOR HOMOPHILIC ADHESION

Summary for 1BIH

• Entry DOI: 10.2210/pdb1bih/pdb
• Descriptor: HEMOLIN, PHOSPHATE ION (2 entities in total)
• Functional Keywords: insect immunity, lps-binding, homophilic adhesion
• Biological source: Hyalophora cecropia (cecropia moth)
• Cellular location: Secreted, extracellular space: P25033
• Total number of polymer chains: 2
• Total formula weight: 88081.16

Authors

Su, X.-D.,Gastinel, L.N.,Vaughn, D.E.,Faye, I.,Poon, P.,Bjorkman, P.J. (deposition date: 1998-06-17, release date: 1998-10-14, Last modification date: 2024-11-13)

Primary citation

Su, X.D.,Gastinel, L.N.,Vaughn, D.E.,Faye, I.,Poon, P.,Bjorkman, P.J.
Crystal structure of hemolin: a horseshoe shape with implications for homophilic adhesion.
Science, 281:991-995, 1998

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.

PubMed: 9703515
DOI: 10.1126/science.281.5379.991

Experimental method

X-RAY DIFFRACTION (3.1 Å)