SSGCID Year IX
EMSL Project ID
49153
Abstract
As witnessed by the recent outbreak of Ebola in Africa, 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
2015-11-09
End Date
2016-09-30
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
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
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
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
Accurate de novo design of hyperstable constrained peptides
Bhardwaj G ,Mulligan V K,Bahl C D,Gilmore J M,Harvey P ,Cheneval O ,Buchko G W,Pulavarti S V,Kass Q ,Eletsky A ,Huang PS ,Johnsen W A,Griesen P ,Rocklin G J,Song Y ,Linsky T W,Watkins A ,Rettie S A,Carter L P,Bonneau R A,Olsen J M,Coutsias E ,Correnti C E,Szyperski T ,Craik D J,Baker D 2016. "Accurate de novo design of hyperstable constrained peptides" Nature 538(7625):329-335. 10.1038/nature19791