Susan Taylor, UCSD, to speak at GTCbio's 11th Protein Kinases in Drug Discovery Conference
Susan Taylor, Professor at UCSD will speak on "Dynamic Assembly and Regulation of Protein Kinases: Spines, Scaffolds and Catalysts" at 11th Protein Kinases in Drug Discovery Conference.
- (1888PressRelease) February 29, 2016 - Dr. Taylor, a protein chemist and structural biologist, received her B.A. from the University of Wisconsin, Madison and her Ph.D. from the Johns Hopkins University with Edward Heath. Rising from the rank of Assistant Professor in Residence in the Chemistry Department to full Professor of Chemistry and Biochemistry (1985) and Professor of Pharmacology in (2004), her research led to solving the crystal structure of the first protein kinase in 1991, providing a template for this entire family of essential regulatory enzymes. Understanding the molecular basis for function, visualizing this one protein kinase and its structure, function and dynamics and translating that information to other related protein kinases continues to provide an ideal interdisciplinary system for coupling technological advances in computation and biophysics with exciting biological questions.
In Dr. Taylor's presentation, "Dynamic Assembly and Regulation of Protein Kinases: Spines, Scaffolds and Catalysts", she states:
Although it has been 25 years since the first protein kinase structure was solved, we still are learning much about the fundamental properties that define this large family of enzymes that regulate so much of biology, and cAMP-dependent protein kinase (PKA) continues to serve as a prototype that drives our understanding. An important concept emerged when we compared active and inactive protein kinases and discovered a hydrophobic core architecture that is dynamically assembled and conserved in every active kinase. The characteristic feature of an active kinase is a hydrophobic regulatory spine (R-spine) that consists of four aligned residues. The assembly of the R-spine is highly regulated and dynamic. A second spine, referred to as the catalytic spine (C-spine), is completed by the adenine ring of ATP and allows for the two lobes of the kinase core, the N-lobe and the C-lobe, to work in synchrony. Both spines are anchored to the unusual hydrophobic αF-helix that spans the C-lobe. The spine hypothesis has been recently validated, in collaboration with Andrey Shaw (Washington University/Genentech), using BRAF as a model system where we show that many Leu-to-Phe mutations can either strengthen the R-spine or facilitate ordering of the αC-Helix to create constitutively active BRAFs that hijack the normal regulatory process. Many of these mutations are found in cancer genomes. C-spine mutations, on the other hand, can create kinase dead mutants that can no longer bind ATP but nevertheless have an "active-like" scaffold that can mediate the downstream activation of MEK and ERK. As a second independent validation of the spine hypothesis, in collaboration with G. Veglia (University of Minnesota), we use NMR to show that residues that comprise the extended spine architecture move in synchrony following the addition of ATP. Collectively we discriminate between scaffold and catalytic functions, which introduces new concepts for functional pseudokinases, and confirm that the assembly of the hydrophobic spine is highly dynamic and circumvented by oncogenic mutations. (Funded in part by GM19301, GM100310, and by the Howard Hughes Medical Institute.)
We invite you to attend the 11th Protein Kinases in Drug Discovery Conference, which will take place February 29 - March 1, 2016 in San Diego, CA to listen to Dr. Taylor's talk and many other leaders in the field including Tony Hunter from Salk Institute and Jack Taunton from UCSF!
This conference is also part of the Enzymes in Drug Discovery Summit, which features the following four conferences
1) 11th Protein Kinases in Drug Discovery
2) 6th Ubiquitin Research & Drug Discovery
3) 2nd Protease Inhibitors in Drug Discovery
4) Epigenetic Enzymes in Drug Discovery
For more information, please visit www.gtcbio.com/pkdd or contact us using the information below.
GTCbio
635 W. Foothill Blvd
Monrovia, CA 91016
www.gtcbio.com/
Email: infogtcbio ( @ ) gtcbio dot com
Phone: (626) 256-6405
Fax: (626) 466-4433
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