1o70
From Proteopedia
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'''NOVEL FOLD REVEALED BY THE STRUCTURE OF A FAS1 DOMAIN PAIR FROM THE INSECT CELL ADHESION MOLECULE FASCICLIN I''' | '''NOVEL FOLD REVEALED BY THE STRUCTURE OF A FAS1 DOMAIN PAIR FROM THE INSECT CELL ADHESION MOLECULE FASCICLIN I''' | ||
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[[Category: Hohenester, E.]] | [[Category: Hohenester, E.]] | ||
[[Category: Tisi, D.]] | [[Category: Tisi, D.]] | ||
| - | [[Category: | + | [[Category: Axon guidance]] |
| - | [[Category: | + | [[Category: Cell adhesion]] |
| - | [[Category: | + | [[Category: Corneal dystrophy]] |
| - | [[Category: | + | [[Category: Extracellular module]] |
| - | [[Category: | + | [[Category: Genetic disorder]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:27:45 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 00:27, 3 May 2008
NOVEL FOLD REVEALED BY THE STRUCTURE OF A FAS1 DOMAIN PAIR FROM THE INSECT CELL ADHESION MOLECULE FASCICLIN I
Overview
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.
About this Structure
1O70 is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
Reference
Novel fold revealed by the structure of a FAS1 domain pair from the insect cell adhesion molecule fasciclin I., Clout NJ, Tisi D, Hohenester E, Structure. 2003 Feb;11(2):197-203. PMID:12575939 Page seeded by OCA on Sat May 3 03:27:45 2008
