Journal
STRUCTURE
Volume 11, Issue 2, Pages 197-203Publisher
CELL PRESS
DOI: 10.1016/S0969-2126(03)00002-9
Keywords
cell adhesion; axon guidance; extracellular module; genetic disorder; corneal dystrophy; X-ray crystallography
Funding
- Wellcome Trust [054334] Funding Source: Medline
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Fasciclin I is an insect neural cell adhesion molecule consisting of four FAS1 domains, homologs of which are present in many bacterial, plant, and animal proteins. The crystal structure of FAS1 domains 3 and 4 of Drosophila fasciclin I reveals a novel domain fold, consisting of a seven-stranded beta wedge and a number of alpha helices. The two domains are arranged in a linear fashion and interact through a substantial polar interface. Missense mutations in the FAS1 domains of the human protein betaig-h3 cause corneal dystrophies. Many mutations alter highly conserved core residues, but the two most common mutations, affecting Arg-124 and Arg-555, map to exposed alpha-helical regions, suggesting reduced protein solubility as the disease mechanism.
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