MEDIA RELEASE PR37529
Research Led by Co-founders of aTyr Pharma Illustrates Mechanism for Multifunctionality
of a Single Protein
SAN DIEGO, Dec. 14 /PRNewswire-AsiaNet/ --
Publication in Nature Structural Biology Highlights Structural
Basis for New Biological Activities with Therapeutic Potential
Research published in the December 13, 2009 edition of Nature Structural
Biology uncovers the structural basis for the multifunctionality of aminoacyl
tRNA synthetases. Aminoacyl tRNA synthetases are universal and essential
enzymes of protein synthesis machinery found in all organisms. However, human
synthetases and naturally occurring variants of these enzymes have additional
activities that are vital to normal functioning of the complex human system
biology, yet remain distinct from the basic protein synthesis activities.
aTyr Pharma's proprietary product generating engine is developing new
biotherapeutics based on the additional functions of tRNA synthetases and
naturally occurring variants that are involved in pathways relevant to
treatment of inflammatory diseases, cancer, metabolic disorders and
neurological disorders.
Professor Xiang-Lei Yang of The Scripps Research Institute (TSRI), a
scientific co-founder of aTyr Pharma, led the team that demonstrated how the
structural mechanism of one form of tryptophanyl tRNA synthetase can inhibit
the formation of new blood vessels. According to Paul Schimmel, Professor at
TSRI, co-founder of aTyr Pharma and co-author on the paper, "Many groups have
conducted research on the structural basis of the protein synthesis
activities of tRNA synthetases, but this work published in Nature Structural
Biology is among the first to show how one, single protein can have
completely different activities and functions in humans, depending on where
the activity takes place. It is fascinating to see how a structural feature
required for a protein synthesis activity inside the cell is co-opted to
disrupt a critical binding activity outside the cell."
According to Jeff Watkins, CEO of aTyr Pharma, "In the past few years,
the laboratories of Professors Yang and Schimmel have established a whole new
area of biological research: novel functions of naturally occurring proteins
resected from ancient proteins such as tRNA synthetases. aTyr Pharma's
portfolio capitalizes on this new area of biology by using these naturally
occurring proteins - and their previously unknown roles - to treat a wide
variety of diseases. Uncovering the structural basis for the binding of
resectins to natural ligands on human cells is an important step in
determining how resectins can be used therapeutically, and we are happy that
scientists from aTyr Pharma could contribute to this publication." Scientists
at aTyr Pharma contributing to this paper include Rajesh Belani, Chulho Park,
Eva Armour, Min-Ha Do and Leslie Nangle.
The Nature Structural Biology publication can be accessed at:
SOURCE: aTyr Pharma
CONTACT: Cheryl Quinn,
Director of Business Development of aTyr Pharma,
+1-858-731-8390,
cquinn@atyrpharma.com; or
Media,
Jennifer James of Alta Partners,
+1-415-362-4022,
jjames@altapartners.com
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