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Message: Trying to access array offset on value of type null
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Severity: Warning
Message: Trying to access array offset on value of type null
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Filename: models/Detail_model.php
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File: /var/www/html/application/models/Detail_model.php
File: /var/www/html/application/controllers/Detail.php
File: /var/www/html/index.php
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Filename: helpers/my_audit_helper.php
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File: /var/www/html/application/helpers/my_audit_helper.php
File: /var/www/html/application/controllers/Detail.php
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Filename: controllers/Detail.php
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Backtrace:
File: /var/www/html/application/controllers/Detail.php
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File: /var/www/html/application/controllers/Detail.php
File: /var/www/html/application/controllers/Detail.php
File: /var/www/html/index.php
Novel fold revealed by the structure of a FAS1 domain pair from the insect cell adhesion molecule fasciclin I. | LitMetric
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.
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