STRUCTURAL STUDIES OF HUMAN SERYL-TRNA SYNTHETASE IN ANGIOGENESIS

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Human seryl-tRNA synthetase(SerRS), a class II aminoacyl?tRNA synthetase and an essential enzyme of the translational pathway, was found to be associated with in vascular development and angiogenesis. The body?s loss of control over angiogenesis causes more than 70 major health conditions affecting over one billion people worldwide. Insufficient formation of new blood vessels (angiogenesis) is connected to coronary artery disease, stroke, and chronic wounds. On the other hand, excessive angiogenesis is also detrimental, and linked to conditions such as cancer, diabetic blindness, age-related macular degeneration, rheumatoid arthritis, and psoriasis. Recently, SerRS was found to play an essential role in angiogenesis through VEGFA/VEGFR2 signal pathways. The crystal structures of human SerRS, and of SerRS in complex with its potential interaction partners would provide important mechanistic understandings of a tRNA synthetase in angiogenesis regulation.