Expression and characterization of the olfactomedin domain of human myocilin.

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 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.
Authors	Ildikó Nagy, Mária Trexler, László Patthy
Journal	Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 302 Issue 3 Pg. 554-61 (Mar 14 2003) ISSN: 0006-291X [Print] United States
PMID	12615070 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References	Cytoskeletal Proteins Disulfides Extracellular Matrix Proteins Eye Proteins Glycoproteins Immunoglobulins Lectins Nerve Tissue Proteins olfactomedin trabecular meshwork-induced glucocorticoid response protein Cysteine
Topics	Amino Acid Sequence Animals Circular Dichroism Cysteine (chemistry, metabolism) Cytoskeletal Proteins Disulfides (metabolism) Electrophoresis, Polyacrylamide Gel Extracellular Matrix Proteins (chemistry) Eye Proteins (chemistry, metabolism) Glaucoma (metabolism) Glycoproteins (chemistry, metabolism) Humans Immunoglobulins (metabolism) Lectins (metabolism) Models, Genetic Molecular Sequence Data Mutation Nerve Tissue Proteins (metabolism) Open Reading Frames Pichia (metabolism) Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Sequence Homology, Amino Acid

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