June 2015
Volume 56, Issue 7
Free
ARVO Annual Meeting Abstract  |   June 2015
Molecular structures of olfactomedin domains from different subfamilies
Author Affiliations & Notes
  • Raquel L Lieberman
    School of Chemistry & Biochemistry, Georgia Institute of Technology, Atlanta, GA
  • Shannon Hill
    School of Chemistry & Biochemistry, Georgia Institute of Technology, Atlanta, GA
  • Rebecca K Donegan
    School of Chemistry & Biochemistry, Georgia Institute of Technology, Atlanta, GA
  • Elaine Nguyen
    School of Chemistry & Biochemistry, Georgia Institute of Technology, Atlanta, GA
  • Footnotes
    Commercial Relationships Raquel Lieberman, None; Shannon Hill, None; Rebecca Donegan, None; Elaine Nguyen, None
  • Footnotes
    Support None
Investigative Ophthalmology & Visual Science June 2015, Vol.56, 5525. doi:
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      Raquel L Lieberman, Shannon Hill, Rebecca K Donegan, Elaine Nguyen; Molecular structures of olfactomedin domains from different subfamilies. Invest. Ophthalmol. Vis. Sci. 2015;56(7 ):5525.

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      © ARVO (1962-2015); The Authors (2016-present)

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Abstract

Purpose: Olfactomedin (OLF) domains comprise a large family of proteins found throughout the body, predominantly within extracellular multidomain proteins, that are involved in aspects of development. Even though they have been implicated in a range of disorders, most prominently glaucoma, but also cancers, childhood obesity, inflammatory bowel disease, and attention deficit disorder, little is known about their structure and specific biological function. The purpose of the study was to crystallize and solve the molecular structures of OLF domains from different phylogenetic subfamilies.

Methods: Recombinant expression and purification of OLF domains, their crystallization, X-ray diffraction data collection, structure solution, model building, and refinement.

Results: Crystal structures of three different OLFs were each solved to ~2 Å resolution, revealing the overall architecture and precise location of every amino acid in the domain, as well as surface charges, hydrophilic channels, calcium, and location of other ions.

Conclusions: The structures significantly expand our appreciation of the physicochemical diversity of the OLF domain, and support a biological function involving protein-protein or protein-ligand interactions common to the broader propeller structural class.

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