| First Author | Nagy I | Year | 2003 |
| Journal | Biochem Biophys Res Commun | Volume | 302 |
| Issue | 3 | Pages | 554-61 |
| PubMed ID | 12615070 | Mgi Jnum | J:82557 |
| Mgi Id | MGI:2653665 | Doi | 10.1016/s0006-291x(03)00198-0 |
| Citation | Nagy I, et al. (2003) Expression and characterization of the olfactomedin domain of human myocilin. Biochem Biophys Res Commun 302(3):554-61 |
| abstractText | 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 beta-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. |
