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1o70
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(New page: 200px<br /> <applet load="1o70" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o70, resolution 2.60Å" /> '''NOVEL FOLD REVEALED...)
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Revision as of 19:26, 29 October 2007
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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] with SO4 as [ligand]. 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 Mon Oct 29 21:31:09 2007
