1O70
Novel Fold Revealed by the Structure of a FAS1 Domain Pair from the Insect Cell Adhesion Molecule Fasciclin I
Summary for 1O70
| Entry DOI | 10.2210/pdb1o70/pdb |
| Descriptor | FASCICLIN I, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | cell adhesion, axon guidance, extracellular module, genetic disorder, corneal dystrophy |
| Biological source | DROSOPHILA MELANOGASTER (FRUIT FLY) |
| Total number of polymer chains | 1 |
| Total formula weight | 37301.79 |
| Authors | Clout, N.J.,Tisi, D.,Hohenester, E. (deposition date: 2002-10-23, release date: 2003-02-13, Last modification date: 2024-11-13) |
| Primary citation | Clout, N.J.,Tisi, D.,Hohenester, E. Novel Fold Revealed by the Structure of a Fas1 Domain Pair from the Insect Cell Adhesion Molecule Fasciclin I Structure, 11:197-, 2003 Cited by PubMed Abstract: 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. PubMed: 12575939DOI: 10.1016/S0969-2126(03)00002-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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