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• W2037264457 abstract "The olfactomedin-domain has been first identified in olfactomedin, an extracellular matrix protein of the olfactory neuroepithelium. Members of this extracellular domain-family have since been shown to be present in several metazoan proteins, such as latrophilins, myocilins, and noelins, but their biological function is unknown. The olfactomedin-domain of myocilin is of considerable interest, since mutations affecting this domain are associated with primary open angle glaucoma. In order to define structural features of this domain-type we have expressed the olfactomedin-domain of human myocilin in Pichia pastoris. The olfactomedin-domain contains a single disulphide-bond connecting Cys-245 and Cys-433 residues; secondary structure predictions and circular dichroism studies indicate that it consists primarily of β-strands. It is noteworthy that the majority of mutations associated with severe forms of glaucoma affect residues that reside in conserved secondary structural elements of the olfactomedin-domain or are otherwise critical for the integrity of this protein-fold." @default.
• W2037264457 created "2016-06-24" @default.
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• W2037264457 date "2003-03-01" @default.
• W2037264457 modified "2023-10-10" @default.
• W2037264457 title "Expression and characterization of the olfactomedin domain of human myocilin" @default.
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• W2037264457 doi "https://doi.org/10.1016/s0006-291x(03)00198-0" @default.
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