E-Newsletter
August 2011 Newsletter
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Dear Colleagues Welcome to the summer edition of our newsletter. Collaboration is part of our culture at Emerald, and in this spirit we hope you’ll plan to join us online for a new webinar series that we are launching this month. We think that topics like Fragment Screening, Structural Genomics, Membrane Proteins and others will provide the basis for interesting and informative discussion. In this issue we’re also proud to share progress made by some of our collaborators and by the team involved in the Seattle Structural Genomics Center for Infectious Disease as we push toward the goal of depositing 500 novel structures in the Protein Data Bank to help inspire new therapies in this important area (see “Collaborations”). We’d love to talk about collaborating to accelerate your leads development or biologics engineering project – just call our Business Development office at 206-780-8959.
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The Emerald webinar series will feature speakers who are recognized experts in their fields, drawn from our own staff, and from collaborators and the scientific community at large. We’re planning to build on themes that can’t be covered in one session (e.g., membrane proteins) and to cover timely and hot topics-of-the-day. We welcome your ideas and suggestions, so please drop a note to your host, Doug Davies, and let us know what you think. Mark your calendars and click through for your e-registrations
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New Clinical Candidates
360th Structure Solved in SSGCID
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CORPORATE UPDATES
Integrated NMR Services
ChemDiv Collaboration |
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So far in 2011, Emerald staff has authored or co-authored the following publications:
Discovery of S-nitrosoglutathione reductase inhibitors: Potential agents for the treatment of asthma and other inflammatory diseases Protein crystal structures determined at Emerald BioStructures have supported the advancement of collaborator N30’s N6022, which is currently in clinical development as a potential agent for the treatment of acute asthma. Their investigational new drug is the first GSNOR inhibitor to enter human clinical development.
Predicting the success of fragment screening by X-ray crystallography Scientists from Emerald BioStructures were invited to write two chapters for this volume of Methods in Enzymology, entitled “Fragment Based Drug Design – Tools, Practical Approaches, and Examples.” In this chapter, a survey was conducted across 18 unique fragment-screening campaigns to analyze trends and establish methods for predicting success in fragment screening.
Fragment screening of infectious disease targets in a structural genomics environment This chapter provides a detailed protocol for conducting fragment-based screening by X-ray crystallography for the Seattle Structural Genomics Center for Infectious Disease (http://www.ssgcid.org). It also details two case studies that show the utility in conducting fragment screening within a structural genomics context, both to help annotate (or correct) putative protein function, and to generate novel starting points for drug design.
Unswitch-ABL drugs overcome resistance in chronic myeloid leukemia ABL inhibitors have revolutionized the clinical management of chronic myeloid leukemia, but the BCR-ABLT315I mutation confers resistance to currently approved drugs. Chan et al. show, in this issue of Cancer Cell, that switch-control inhibitors block BCR-ABLT315I activity by preventing ABL from switching from the inactive to active conformation.
SAD phasing using iodide ions in a high-throughput structural genomics We have adopted the use of iodide ion soaks and single wavelength anomalous dispersion (SAD) experiments as our primary method for de novo phasing. This method uses existing native crystals and in house data collection, resulting in rapid, low cost structure determination. Here we present a general overview of this method as well as several examples including SAD phasing of proteins with novel folds and the combined use of SAD and MR for targets with weak MR solutions.
Leveraging structure determination with fragment screening for infectious disease drug targets: MECP synthase from Burkholderia pseudomallei
Crystal structure of a DNA containing the planar, phenoxazine-derived bi-functional spectroscopic probe Ç Scientists at Emerald BioStructures determined a high resolution crystal structure of a DNA containing a modified nucleotide that is a novel, bi-functional spectroscopic probe. The results stem from collaborations with the University of Iceland, the University of St. Andrews, and the Fred Hutchinson Cancer Research Center.
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©2011 Emerald BioStructures. All rights reserved. CrystalReady, Fragments of Life, and Gene Composer are trademarks of Emerald BioStructures. Other trademarks are property of their respective owners
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