1bih
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1bih" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bih, resolution 3.10Å" /> '''CRYSTAL STRUCTURE OF...)
Next diff →
Revision as of 09:33, 20 November 2007
|
CRYSTAL STRUCTURE OF THE INSECT IMMUNE PROTEIN HEMOLIN: A NEW DOMAIN ARRANGEMENT WITH IMPLICATIONS FOR HOMOPHILIC ADHESION
Overview
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.
About this Structure
1BIH is a Single protein structure of sequence from Hyalophora cecropia with PO4 as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of hemolin: a horseshoe shape with implications for homophilic adhesion., Su XD, Gastinel LN, Vaughn DE, Faye I, Poon P, Bjorkman PJ, Science. 1998 Aug 14;281(5379):991-5. PMID:9703515
Page seeded by OCA on Tue Nov 20 11:40:48 2007
