Seattle Structural Genomics Center for Infectious Disease (SSGCID) -- Year X
EMSL Project ID
49703
Abstract
As witnessed by the recent Zika virus scare, developing new drugs to combat emerging and re-emerging infectious diseases is of upmost importance. The National Institute of Allergy and Infectious Diseases (NIAID) has identified the need to prepare a library of three-dimensional protein structures of potential drug targets that may be used for the structure-based design of new drugs. Towards populating this library NIAID has established two structural genomics centers: The Center for Structural Genomics of Infectious Disease (CSGID) and the Seattle Structural Genomics Center for Infectious Disease (SSGCID). The high-field suite of NMR spectrometers at EMSL will assist the population of the structure library with the high-field NMR data used to determine the solution structure for 2-3 proteins identified as potential drug targets.
Project Details
Start Date
2016-12-05
End Date
2017-09-30
Status
Closed
Released Data Link
Team
Principal Investigator
Related Publications
Buchko G.W., J. Abendroth, J.I. Robinson, I. Phan, P.J. Myler, and T.E. Edwards. 2020. "Structural diversity in the mycobacteria DUF3349 superfamily." Protein Science 29, no. 3:670-685. PNNL-SA-147115. doi:10.1002/pro.3758
Buchko GW, N Echols, EM Flynn, HL Ng, S Stephenson, H Kim, PJ Myler, TC Terwilliger, T Alber, and CY Kim. 2017. "Structural and biophysical characterization of the Mycobacterium tuberculosis protein Rv0577, a protein associated with neutral red staining of virulent tuberculosis strains and homologue of the Streptomyces coelicolor protein KbpA." Biochemistry 56(30):4015-4027. doi:10.1021/acs.biochem.7b00511
Buchko G.W., R.M. Jayasinha Arachchige, J. Tao, B.J. Tarasevich, and W.J. Shaw. 2018. "Identification of major metalloproteinase-20 proteolytic processing products of murine amelogenin and tyrosine-rich amleogenin peptide using a nuclear magnetic resonance spectroscopy based method." Archives of Oral Biology 93, no. 1:187-194. PNNL-SA-132678. doi:10.1016/j.archoralbio.2018.06.001
Buchko G.W., S.N. Hewitt, W.C. Van Voorhis, and P.J. Myler. 2018. "Solution NMR Structures of Oxidized and Reduced Ehrlichia chaffeensis thioredoxin: NMR-Invisible Structure Owing to Backbone Dynamics." Acta Crystallographica. Section F 74, no. 1:46-56. PNNL-SA-126464. doi:10.1107/S2053230X1701799X
Buchko G.W., S.V. Pulavarti, V. Ovchinnikov, E.A. Shaw, S.A. Rettie, P.J. Myler, and M. Karplus, et al. 2018. "Cytosolic expression, solution structures, and molecular dynamics simulation of genetically encodable disulfide-rich de novo designed peptides." Protein Science 27, no. 9:1611-1623. PNNL-SA-129358. doi:10.1002/pro.3453
Elnaas A.R., D. Grice, J. Han, Y. Feng, A. Di Capau, T. Mak, and J.A. Laureanti, et al. 2020. "Discovery of a Natural Product that Binds to the Mycobacterium tuberculosis Protein Rv1466 by Native Mass Spectrometry." Molecules 25, no. 10:2384. PNNL-SA-152797. doi:10.3390/molecules25102384
Ma Z., J. Abendroth, G.W. Buchko, K.H. Rohde, and V.L. Davidson. 2020. "Crystal structure of a hemerythrin-like protein from Mycobacterium kansasii and homology model of the orthologous Rv2633c protein of M. tuberculosis." Biochemical Journal 477, no. 2:567-581. PNNL-SA-147766. doi:10.1042/BCJ20190827
Shaheen S., K.F. Barrett, S. Subramanian, S.L. Arnold, J.A. Laureanti, P.J. Myler, and W.C. Van Voorhis, et al. 2020. "Solution structure for an Encephalitozoon cuniculi adrenodoxin-like protein in the oxidized state." Protein Science 29, no. 3:809-817. PNNL-SA-150252. doi:10.1002/pro.3818
Xie Y., Y. Feng, A. Di Capua, T. Mak, G.W. Buchko, P.J. Myler, and M. Lui, et al. 2020. "A Phenotarget Approach for Identifying an Alkaloid Interacting with the Tuberculosis Protein Rv1466." Marine Drugs 18, no. 3:149. PNNL-SA-150251. doi:10.3390/md18030149