Structural biologists map the architecture of individual proteins as well as multi-protein complexes and use that information to understand the structure, function, and dynamic interactions of those proteins and complexes. At atomic and molecular resolutions, structural data help scientists rationally design new molecules that selectively modulate the activity of particular proteins. Such inhibitors or activators serve as research tools that allow investigators to study protein activity in living cells or can, in some cases, be developed into new drugs to treat human disease in a targeted manner. Researchers in these areas at Einstein has made considerable investments in instrumentation and infrastructure to build a state-of-the-art program in structural biology using NMR, and a 16 y old instrument is seriously in need of upgrading to contemporary performance and reliability. The upgrade of the console controller and probe for signal detection will increase the throughput for this instrument by more than four fold. The 10 major users and many other users in structural biology, enzymology, and chemical biology will be significantly aided in their NIH funded research in multiple areas of disease and therapeutics. Specific areas include antimicrobials, cancer therapeutics for tumor metastasis, antivirals, cardiac degeneration, Alzheimer's, and reproductive health.

Agency
National Institute of Health (NIH)
Institute
Office of The Director, National Institutes of Health (OD)
Type
Biomedical Research Support Shared Instrumentation Grants (S10)
Project #
1S10OD016305-01A1
Application #
8640531
Study Section
Special Emphasis Panel (ZRG1)
Program Officer
Levy, Abraham
Project Start
2014-07-01
Project End
2015-06-30
Budget Start
2014-07-01
Budget End
2015-06-30
Support Year
1
Fiscal Year
2014
Total Cost
Indirect Cost
Name
Albert Einstein College of Medicine
Department
Biochemistry
Type
Schools of Medicine
DUNS #
City
Bronx
State
NY
Country
United States
Zip Code
10461
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Wang, Ting; Cook, Ian; Leyh, Thomas S (2017) The NSAID allosteric site of human cytosolic sulfotransferases. J Biol Chem 292:20305-20312
Upla, Paula; Kim, Seung Joong; Sampathkumar, Parthasarathy et al. (2017) Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex. Structure 25:434-445
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Uchime, Onyinyechukwu; Dai, Zhou; Biris, Nikolaos et al. (2016) Synthetic Antibodies Inhibit Bcl-2-associated X Protein (BAX) through Blockade of the N-terminal Activation Site. J Biol Chem 291:89-102
Xia, Yumin; Eryilmaz, Ertan; Zhang, Qiuting et al. (2016) Anti-DNA antibody mediated catalysis is isotype dependent. Mol Immunol 69:33-43
Cook, Ian; Wang, Ting; Girvin, Mark et al. (2016) The structure of the catechin-binding site of human sulfotransferase 1A1. Proc Natl Acad Sci U S A 113:14312-14317
Garner, Thomas P; Reyna, Denis E; Priyadarshi, Amit et al. (2016) An Autoinhibited Dimeric Form of BAX Regulates the BAX Activation Pathway. Mol Cell 63:485-97

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