Research Led By Co-founders Of Atyr Pharma Illustrates Mechanism For Multifunctionality Of A Single

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15th December 2009, 01:19am - Views: 1113

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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, 

Culture International ATyr Pharma 3 image

             Director of Business Development of aTyr Pharma,


   ; or 


             Jennifer James of Alta Partners, 




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