Seattle Structural Genomics Center for Infectious Diseases – Year XI
EMSL Project ID
50089
Abstract
A potential consequence of rapid climate change is the emergence of epidemic infectious zoonotic diseases as the habitats of disease carriers change to expose human populations to new infectious agents. These environmental changes, along with the emergence of multi-drug resistant strains, makes developing new drugs to combat emerging and re-emerging infectious diseases 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
2017-10-23
End Date
2018-09-30
Status
Closed
Released Data Link
Team
Principal Investigator
Related Publications
Discovery of a Natural Product That Binds to the Mycobacterium tuberculosis Protein Rv1466 Using Native Mass Spectrometry
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
A Phenotarget Approach for Identifying an Alkaloid Interacting with the Tuberculosis Protein Rv1466
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
Structural diversity in the Mycobacteria DUF3349 superfamily
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
Solution structure for an Encephalitozoon cuniculi adrenodoxin‐like protein in the oxidized state
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
Crystal structure of a hemerythrin-like protein from Mycobacterium kansasii and homology model of the orthologous Rv2633c protein of M. tuberculosis
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
Cytosolic expression, solution structures, and molecular dynamics simulation of genetically encodable disulfide‐rich de novo designed peptides
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
Solution NMR structures of oxidized and reducedEhrlichia chaffeensisthioredoxin: NMR-invisible structure owing to backbone dynamics
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