1BIH

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

1BIH の概要

• エントリーDOI: 10.2210/pdb1bih/pdb
• 分子名称: HEMOLIN, PHOSPHATE ION (2 entities in total)
• 機能のキーワード: insect immunity, lps-binding, homophilic adhesion
• 由来する生物種: Hyalophora cecropia (cecropia moth)
• 細胞内の位置: Secreted, extracellular space: P25033
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 88081.16

構造登録者

Su, X.-D.,Gastinel, L.N.,Vaughn, D.E.,Faye, I.,Poon, P.,Bjorkman, P.J. (登録日: 1998-06-17, 公開日: 1998-10-14, 最終更新日: 2018-03-07)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.1 Å)