The Northeast Structural Genomics Consortium (NESG) is one of four Large-Scale Centers (LSCs) for structure production funded by the NIH NIGMS Protein Structure Initiative (PSI). The goals of the PSI LSCs are to (i) generate three-dimensional (3D) structures for large numbers of proteins selected using broad biological, genomic, and bioinformatics criteria, together with targets selected from specific biological theme projects, so as to provide significant structural coverage of a large number of protein sequences In nature, (ii) develop and disseminate novel and/or improved technologies for structural biology and bioinformatics, and (iii) make these structures, structure production data, and the associated reagents and technologies publicly available to the worldwide scientific community. In PSI:Biology, the next phase of the PSI program, the NESG will expand Its mission by carrying our collaborative structural genomics projects together with several PSI Consortia for High-Through-Put (HTP) Enabled Structural Biology Partnerships (Biology Partnerships) and associated Program Announcements (PARs). The primary goal of the NESG In PSI:Biology is to provide >1,100 new 3D protein structures to the Protein Data Bank (PDB) over 5 years, together with extensive raw and processed data, protocols for sample production, structure/function annotations, and thousands of homology models derived from these structures. This will complement the ~ 900 structures deposited by NESG in PSI Phases 1 and 2. In particular, NESG will provide novel 3D structural information useful in modeling large numbers of eukaryotic and human proteins. Our efforts will span five classes of target types: (i) proteins nominated In collaborations to be established with PSI Biology Partnerships, (ii) domain families (referred to as BIG, MEGA, and META families) defined by the central PSI:Biology Target Selection Subcommittee to provide course-grained coverage of large protein domain families;(iii) proteins defined by the NESG Biomedical Theme of 'Networks of Proteins Associated with Human Cancer and Developmental Biology';(iv) proteins nominated by the general biomedical research community, and (v) proteins selected for specific technology-development goals. Protein targets in the first two of these classes, representing ~ 80% of the overall NESG effort, will be selected in a coordinated process together with the other LSCs and Biology Partnerships so as to maximize biological impact and minimize redundant efforts. The many methods and technologies for structural genomics research developed in this project will provide the next- generation tools for traditional hypothesis-driven biological research, and will thus have powerful and broad impact on the infrastructure for biological science and engineering.
The NESG consortium will make 3D structural information a routinely and broadly used component of biological research. The proposed program includes plans for training young scientists. We will provide structural coverage of hundreds of human proteins associated with cancer and developmental biology, as well as coverage of many eukaryotic protein domain families. This discovery research program will generate new technologies and novel specific biomedical hypotheses, along with the information and reagents needed for follow on functional studies, providing the basis for new R01-type research programs.
|Zhang, Meng; Yu, Xiao-Wei; Swapna, G V T et al. (2016) Efficient production of (2)H, (13)C, (15)N-enriched industrial enzyme Rhizopus chinensis lipase with native disulfide bonds. Microb Cell Fact 15:123|
|Jacobs, T M; Williams, B; Williams, T et al. (2016) Design of structurally distinct proteins using strategies inspired by evolution. Science 352:687-90|
|Adams, Paul D; Aertgeerts, Kathleen; Bauer, Cary et al. (2016) Outcome of the First wwPDB/CCDC/D3R Ligand Validation Workshop. Structure 24:502-8|
|BoÃ«l, GrÃ©gory; Letso, Reka; Neely, Helen et al. (2016) Codon influence on protein expression in E. coli correlates with mRNA levels. Nature 529:358-63|
|Ma, Li-Chung; Guan, Rongjin; Hamilton, Keith et al. (2016) A Second RNA-Binding Site in the NS1 Protein of Influenza B Virus. Structure 24:1562-72|
|Cai, Kai; Liu, Gaohua; Frederick, Ronnie O et al. (2016) Structural/Functional Properties of Human NFU1, an Intermediate [4Fe-4S] Carrier in Human Mitochondrial Iron-Sulfur Cluster Biogenesis. Structure 24:2080-2091|
|Everett, John K; Tejero, Roberto; Murthy, Sarath B K et al. (2016) A community resource of experimental data for NMR / X-ray crystal structure pairs. Protein Sci 25:30-45|
|Bhardwaj, Gaurav; Mulligan, Vikram Khipple; Bahl, Christopher D et al. (2016) Accurate de novo design of hyperstable constrained peptides. Nature 538:329-335|
|Sheng, Ren; Jung, Da-Jung; Silkov, Antonina et al. (2016) Lipids Regulate Lck Protein Activity through Their Interactions with the Lck Src Homology 2 Domain. J Biol Chem 291:17639-50|
|Park, Mi-Jeong; Sheng, Ren; Silkov, Antonina et al. (2016) SH2 Domains Serve as Lipid-Binding Modules for pTyr-Signaling Proteins. Mol Cell 62:7-20|
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