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1o70

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[[Image:1o70.gif|left|200px]]
[[Image:1o70.gif|left|200px]]
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{{Structure
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|PDB= 1o70 |SIZE=350|CAPTION= <scene name='initialview01'>1o70</scene>, resolution 2.60&Aring;
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The line below this paragraph, containing "STRUCTURE_1o70", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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{{STRUCTURE_1o70| PDB=1o70 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o70 OCA], [http://www.ebi.ac.uk/pdbsum/1o70 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1o70 RCSB]</span>
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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.]]
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[[Category: axon guidance]]
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[[Category: Axon guidance]]
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[[Category: cell adhesion]]
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[[Category: Cell adhesion]]
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[[Category: corneal dystrophy]]
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[[Category: Corneal dystrophy]]
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[[Category: extracellular module]]
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[[Category: Extracellular module]]
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[[Category: genetic disorder]]
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[[Category: Genetic disorder]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:27:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:40:46 2008''
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Revision as of 00:27, 3 May 2008

Image:1o70.gif

Template:STRUCTURE 1o70

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

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