1o70
From Proteopedia
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| - | [[Image:1o70.gif|left|200px]]<br /> | + | [[Image:1o70.gif|left|200px]]<br /><applet load="1o70" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1o70" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1o70, resolution 2.60Å" /> | caption="1o70, resolution 2.60Å" /> | ||
'''NOVEL FOLD REVEALED BY THE STRUCTURE OF A FAS1 DOMAIN PAIR FROM THE INSECT CELL ADHESION MOLECULE FASCICLIN I'''<br /> | '''NOVEL FOLD REVEALED BY THE STRUCTURE OF A FAS1 DOMAIN PAIR FROM THE INSECT CELL ADHESION MOLECULE FASCICLIN I'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1O70 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. | + | 1O70 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:So4 Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O70 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: genetic disorder]] | [[Category: genetic disorder]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 16:51:50 2007'' |
Revision as of 14:42, 18 December 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. Known structural/functional Site: . 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
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