Research Highlights

GSQASS segment from the Nucleoprotein of SARS-CoV-2, residues 179-184
Tayeb-Fligelman, E., Bowler, J. T., Tai, C. E., Sawaya, M. R., Jiang, Y. Xiao, Garcia, G., Griner, S. L., Cheng, X., Salwinski, L., Lutter, L., Seidler, P. M., Lu, J., Rosenberg, G. M., Hou, K., Abskharon, R., Pan, H., Zee, C. - T., Boyer, D. R., Li, Y., Anderson, D. H., Murray, K. A., Falcon, G., Cascio, D., Saelices, L., Damoiseaux, R., Arumugaswami, V., Guo, F., and Eisenberg, D. S. (2023) Low complexity domains of the nucleocapsid protein of SARS-CoV-2 form amyloid fibrils. Nat Commun. 14, 2379
Crystal structure of SARS-CoV-2 (Covid-19) Nsp3 macrodomain in complex with TFMU-ADPr
Anmangandla, A., Jana, S., Peng, K., Wallace, S. D., Bagde, S. R., Drown, B. S., Xu, J., Hergenrother, P. J., J Fromme, C., and Lin, H. (2023) A Fluorescence Polarization Assay for Macrodomains Facilitates the Identification of Potent Inhibitors of the SARS-CoV-2 Macrodomain. ACS Chem Biol. 18, 1200-1207
Crystal structure of coxsackievirus B3 cloverleaf RNA replication element
Das, N. K., Hollmann, N. M., Vogt, J., Sevdalis, S. E., Banna, H. A., Ojha, M., and Koirala, D. (2023) Crystal structure of a highly conserved enteroviral 5' cloverleaf RNA replication element. Nat Commun. 14, 1955
7S83
Chen, W. - H., Hajduczki, A., Martinez, E. J., Bai, H., Matz, H., Hill, T. M., Lewitus, E., Chang, W. C., Dawit, L., Peterson, C. E., Rees, P. A., Ajayi, A. B., Golub, E. S., Swafford, I., Dussupt, V., David, S., Mayer, S. V., Soman, S., Kuklis, C., Corbitt, C., King, J., Choe, M., Sankhala, R. S., Thomas, P. V., Zemil, M., Wieczorek, L., Hart, T., Duso, D., Kummer, L., Yan, L., Sterling, S. L., Laing, E. D., Broder, C. C., Williams, J. K., Davidson, E., Doranz, B. J., Krebs, S. J., Polonis, V. R., Paquin-Proulx, D., Rolland, M., Reiley, W. W., Gromowski, G. D., Modjarrad, K., Dooley, H., and M Joyce, G. (2023) Shark nanobodies with potent SARS-CoV-2 neutralizing activity and broad sarbecovirus reactivity. Nat Commun. 14, 580
I-2 Y35N H35N (unbound) Fab from CH65-CH67 lineage
Phillips, A. M., Maurer, D. P., Brooks, C., Dupic, T., Schmidt, A. G., and Desai, M. M. (2023) Hierarchical sequence-affinity landscapes shape the evolution of breadth in an anti-influenza receptor binding site antibody. Elife. 10.7554/eLife.83628
Crystal structure of human METTL1 and WDR4 complex
Li, J., Wang, L., Hahn, Q., Nowak, R. P., Viennet, T., Orellana, E. A., Burman, S. S. Roy, Yue, H., Hunkeler, M., Fontana, P., Wu, H., Arthanari, H., Fischer, E. S., and Gregory, R. I. (2023) Structural basis of regulated mG tRNA modification by METTL1-WDR4. Nature. 613, 391-397
Dalton, K. M., Greisman, J. B., and Hekstra, D. R. (2022) A unifying Bayesian framework for merging X-ray diffraction data. Nat Commun. 13, 7764
Crystal structure of the Thermus thermophilus 70S ribosome in complex with mRNA, aminoacylated A-site Phe-NH-tRNAphe, peptidyl P-site fMSEAC-NH-tRNAmet, and deacylated E-site tRNAphe at 2.40A resolution
Syroegin, E. A., Aleksandrova, E. V., and Polikanov, Y. S. (2022) Insights into the ribosome function from the structures of non-arrested ribosome-nascent chain complexes. Nat Chem. 10.1038/s41557-022-01073-1
Hallucinated C2 protein assembly HALC2_068
Wicky, B. I. M., Milles, L. F., Courbet, A., Ragotte, R. J., Dauparas, J., Kinfu, E., Tipps, S., Kibler, R. D., Baek, M., DiMaio, F., Li, X., Carter, L., Kang, A., Nguyen, H., Bera, A. K., and Baker, D. (2022) Hallucinating symmetric protein assemblies. Science. 378, 56-61
Structure of human TREX1-DNA complex
Zhou, W., Richmond-Buccola, D., Wang, Q., and Kranzusch, P. J. (2022) Structural basis of human TREX1 DNA degradation and autoimmune disease. Nat Commun. 13, 4277
Crystal structure of human TMPRSS2 in complex with Nafamostat
Fraser, B. J., Beldar, S., Seitova, A., Hutchinson, A., Mannar, D., Li, Y., Kwon, D., Tan, R., Wilson, R. P., Leopold, K., Subramaniam, S., Halabelian, L., Arrowsmith, C. H., and Bénard, F. (2022) Structure and activity of human TMPRSS2 protease implicated in SARS-CoV-2 activation. Nat Chem Biol. 10.1038/s41589-022-01059-7
Crystal structure of NPR1
Kumar, S., Zavaliev, R., Wu, Q., Zhou, Y., Cheng, J., Dillard, L., Powers, J., Withers, J., Zhao, J., Guan, Z., Borgnia, M. J., Bartesaghi, A., Dong, X., and Zhou, P. (2022) Structural basis of NPR1 in activating plant immunity. Nature. 605, 561-566
7TTM
Liu, L., Iketani, S., Guo, Y., Casner, R. G., Reddem, E. R., Nair, M. S., Yu, J., Chan, J. F. - W., Wang, M., Cerutti, G., Li, Z., Morano, N. C., Castagna, C. D., Corredor, L., Chu, H., Yuan, S., Poon, V. Kwok- Man, Chan, C. Chun- Sing, Chen, Z., Luo, Y., Cunningham, M., Chavez, A., Yin, M. T., Perlin, D. S., Tsuji, M., Yuen, K. - Y., Kwong, P. D., Sheng, Z., Huang, Y., Shapiro, L., and Ho, D. D. (2022) An antibody class with a common CDRH3 motif broadly neutralizes sarbecoviruses. Sci Transl Med. 10.1126/scitranslmed.abn6859
Crystal structure of SARS-CoV-2 3CL in complex with inhibitor EB46
Liu, H., Iketani, S., Zask, A., Khanizeman, N., Bednarova, E., Forouhar, F., Fowler, B., Hong, S. Jung, Mohri, H., Nair, M. S., Huang, Y., Tay, N. E. S., Lee, S., Karan, C., Resnick, S. J., Quinn, C., Li, W., Shion, H., Xia, X., Daniels, J. D., Bartolo-Cruz, M., Farina, M., Rajbhandari, P., Jurtschenko, C., Lauber, M. A., McDonald, T., Stokes, M. E., Hurst, B. L., Rovis, T., Chavez, A., Ho, D. D., and Stockwell, B. R. (2022) Development of optimized drug-like small molecule inhibitors of the SARS-CoV-2 3CL protease for treatment of COVID-19. Nat Commun. 13, 1891
Structure of SARS-CoV-2 main protease in complex with GC376
Moghadasi, S. Arad, Esler, M. A., Otsuka, Y., Becker, J. T., Moraes, S. N., Anderson, C. B., Chamakuri, S., Belica, C., Wick, C., Harki, D. A., Young, D. W., Scampavia, L., Spicer, T. P., Shi, K., Aihara, H., Brown, W. L., and Harris, R. S. (2022) Gain-of-Signal Assays for Probing Inhibition of SARS-CoV-2 M/3CL in Living Cells. mBio. 10.1128/mbio.00784-22
SARS-CoV-2 Receptor Binding Domain in Complex with Ab17
Hauser, B. M., Sangesland, M., St Denis, K. J., Lam, E. C., Case, J. Brett, Windsor, I. W., Feldman, J., Caradonna, T. M., Kannegieter, T., Diamond, M. S., Balazs, A. B., Lingwood, D., and Schmidt, A. G. (2022) Rationally designed immunogens enable immune focusing following SARS-CoV-2 spike imprinting. Cell Rep. 38, 110561
SARS-CoV-2 S protein RBD in complex with A5-10 Fab
Wang, F., Li, L., Dou, Y., Shi, R., Duan, X., Liu, H., Zhang, J., Liu, D. D., Wu, J., He, Y., Lan, J., Lu, B., Feng, H., and Yan, J. (2022) Etesevimab in combination with JS026 neutralizing SARS-CoV-2 and its variants. Emerg Microbes Infect. 11, 548-551
7MC5
Moeller, N. H., Shi, K., Demir, Ö., Belica, C., Banerjee, S., Yin, L., Durfee, C., Amaro, R. E., and Aihara, H. (2022) Structure and dynamics of SARS-CoV-2 proofreading exoribonuclease ExoN. Proc Natl Acad Sci U S A. 10.1073/pnas.2106379119
Crystal Structure of SARS-CoV-2 Main Protease (3CLpro/Mpro) Covalently Bound to Compound C63
Stille, J. K., Tjutrins, J., Wang, G., Venegas, F. A., Hennecker, C., Rueda, A. M., Sharon, I., Blaine, N., Miron, C. E., Pinus, S., Labarre, A., Plescia, J., Patrascu, M. Burai, Zhang, X., Wahba, A. S., Vlaho, D., Huot, M. J., T Schmeing, M., Mittermaier, A. K., and Moitessier, N. (2022) Design, synthesis and in vitro evaluation of novel SARS-CoV-2 3CL covalent inhibitors.. Eur J Med Chem. 229, 114046
SARS-CoV-2 frameshifting pseudoknot RNA
Jones, C. P., and Ferré-D'Amaré, A. R. (2022) Crystal structure of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) frameshifting pseudoknot. RNA. 10.1261/rna.078825.121
Crystal structure of the SARS-CoV-2 receptor binding domain in complex with VNAR 3B4
Ubah, O. C., Lake, E. W., Gunaratne, G. S., Gallant, J. P., Fernie, M., Robertson, A. J., Marchant, J. S., Bold, T. D., Langlois, R. A., Matchett, W. E., Thiede, J. M., Shi, K., Yin, L., Moeller, N. H., Banerjee, S., Ferguson, L., Kovaleva, M., Porter, A. J., Aihara, H., LeBeau, A. M., and Barelle, C. J. (2021) Mechanisms of SARS-CoV-2 neutralization by shark variable new antigen receptors elucidated through X-ray crystallography. Nat Commun. 12, 7325
Crystal structure of spike protein receptor binding domain of escape mutant SARS-CoV-2 from immunocompromised patient (d146*) in complex with human receptor ACE2
Nabel, K. G., Clark, S. A., Shankar, S., Pan, J., Clark, L. E., Yang, P., Coscia, A., McKay, L. G. A., Varnum, H. H., Brusic, V., Tolan, N. V., Zhou, G., Desjardins, M., Turbett, S. E., Kanjilal, S., Sherman, A. C., Dighe, A., LaRocque, R. C., Ryan, E. T., Tylek, C., Cohen-Solal, J. F., Darcy, A. T., Tavella, D., Clabbers, A., Fan, Y., Griffiths, A., Correia, I. R., Seagal, J., Baden, L. R., Charles, R. C., and Abraham, J. (2021) Structural basis for continued antibody evasion by the SARS-CoV-2 receptor binding domain. Science
7LIR
Li, T., Stayrook, S. E., Tsutsui, Y., Zhang, J., Wang, Y., Li, H., Proffitt, A., Krimmer, S. G., Ahmed, M., Belliveau, O., Walker, I. X., Mudumbi, K. C., Suzuki, Y., Lax, I., Alvarado, D., Lemmon, M. A., Schlessinger, J., and Klein, D. E. (2021) Structural basis for ligand reception by anaplastic lymphoma kinase. Nature. 600, 148-152
7N4I
Dussupt, V., Sankhala, R. S., Mendez-Rivera, L., Townsley, S. M., Schmidt, F., Wieczorek, L., Lal, K. G., Donofrio, G. C., Tran, U., Jackson, N. D., Zaky, W. I., Zemil, M., Tritsch, S. R., Chen, W. - H., Martinez, E. J., Ahmed, A., Choe, M., Chang, W. C., Hajduczki, A., Jian, N., Peterson, C. E., Rees, P. A., Rutkowska, M., Slike, B. M., Selverian, C. N., Swafford, I., Teng, I. - T., Thomas, P. V., Zhou, T., Smith, C. J., Currier, J. R., Kwong, P. D., Rolland, M., Davidson, E., Doranz, B. J., Mores, C. N., Hatziioannou, T., Reiley, W. W., Bieniasz, P. D., Paquin-Proulx, D., Gromowski, G. D., Polonis, V. R., Michael, N. L., Modjarrad, K., M Joyce, G., and Krebs, S. J. (2021) Low-dose in vivo protection and neutralization across SARS-CoV-2 variants by monoclonal antibody combinations. Nat Immunol. 10.1038/s41590-021-01068-z
7RQ8
Mitcheltree, M. J., Pisipati, A., Syroegin, E. A., Silvestre, K. J., Klepacki, D., Mason, J. D., Terwilliger, D. W., Testolin, G., Pote, A. R., J Y Wu, K., Ladley, R. Porter, Chatman, K., Mankin, A. S., Polikanov, Y. S., and Myers, A. G. (2021) A synthetic antibiotic class overcoming bacterial multidrug resistance. Nature. 10.1038/s41586-021-04045-6
7LFV
Patchett, S., Lv, Z., Rut, W., Békés, M., Drag, M., Olsen, S. K., and Huang, T. T. (2021) A molecular sensor determines the ubiquitin substrate specificity of SARS-CoV-2 papain-like protease. Cell Rep. 36, 109754
Structure of the SARS-CoV-2 N protein C-terminal domain bound to single-domain antibody E2
Ye, Q., Lu, S., and Corbett, K. D. (2021) Structural Basis for SARS-CoV-2 Nucleocapsid Protein Recognition by Single-Domain Antibodies. Front Immunol. 12, 719037
SARS-CoV-2 main protease in complex with N-terminal autoprocessing substrate
MacDonald, E. A., Frey, G., Namchuk, M. N., Harrison, S. C., Hinshaw, S. M., and Windsor, I. W. (2021) Recognition of Divergent Viral Substrates by the SARS-CoV-2 Main Protease. ACS Infect Dis. 10.1021/acsinfecdis.1c00237
Crystal structure of the SARS-CoV-2 (2019-NCoV) main protease in complex with 5-(3-{3-chloro-5-[(5-methyl-1,3-thiazol-4-yl)methoxy]phenyl}-2-oxo-2H-[1,3'-bipyridin]-5-yl)pyrimidine-2,4(1H,3H)-dione (compound 13)
Zhang, C. - H., Spasov, K. A., Reilly, R. A., Hollander, K., Stone, E. A., Ippolito, J. A., Liosi, M. - E., Deshmukh, M. G., Tirado-Rives, J., Zhang, S., Liang, Z., Miller, S. J., Isaacs, F., Lindenbach, B. D., Anderson, K. S., and Jorgensen, W. L. (2021) Optimization of Triarylpyridinone Inhibitors of the Main Protease of SARS-CoV-2 to Low-Nanomolar Antiviral Potency. ACS Med Chem Lett. 12, 1325-1332
Crystal structure of SARS-CoV-2 RBD complexed with Nanosota-1
Ye, G., Gallant, J., Zheng, J., Massey, C., Shi, K., Tai, W., Odle, A., Vickers, M., Shang, J., Wan, Y., Du, L., Aihara, H., Perlman, S., LeBeau, A., and Li, F. (2021) The development of Nanosota-1 as anti-SARS-CoV-2 nanobody drug candidates. Elife. 10.7554/eLife.64815
SARS-CoV-2 programmed -1 frameshifting element three stem H-type pseudoknot
Roman, C., Lewicka, A., Koirala, D., Li, N. - S., and Piccirilli, J. A. (2021) The SARS-CoV-2 Programmed -1 Ribosomal Frameshifting Element Crystal Structure Solved to 2.09 Å Using Chaperone-Assisted RNA Crystallography.. ACS Chem Biol. 10.1021/acschembio.1c00324
CRYSTAL STRUCTURE OF THE SARS-COV-2(2019-NCOV) MAIN PROTEASE IN COMPLEX WITH COMPOUND 23
Deshmukh, M. G., Ippolito, J. A., Zhang, C. - H., Stone, E. A., Reilly, R. A., Miller, S. J., Jorgensen, W. L., and Anderson, K. S. (2021) Structure-guided design of a perampanel-derived pharmacophore targeting the SARS-CoV-2 main protease. Structure. 10.1016/j.str.2021.06.002
Structure of SARS-CoV-2 nsp16/nsp10 complex in presence of S-adenosyl-L-homocysteine (SAH)
Viswanathan, T., Misra, A., Chan, S. - H., Qi, S., Dai, N., Arya, S., Martinez-Sobrido, L., and Gupta, Y. K. (2021) A metal ion orients SARS-CoV-2 mRNA to ensure accurate 2'-O methylation of its first nucleotide. Nat Commun. 12, 3287
Structure of human PARG complexed with PARG-292, 7KG7
Brosey, C. A., Houl, J. H., Katsonis, P., Balapiti-Modarage, L. P. F., Bommagani, S., Arvai, A., Moiani, D., Bacolla, A., Link, T., Warden, L. S., Lichtarge, O., Jones, D. E., Ahmed, Z., and Tainer, J. A. (2021) Targeting SARS-CoV-2 Nsp3 macrodomain structure with insights from human poly(ADP-ribose) glycohydrolase (PARG) structures with inhibitors. Prog Biophys Mol Biol. 10.1016/j.pbiomolbio.2021.02.002
CRYSTAL STRUCTURE OF THE SARS-COV-2(2019-NCOV) MAIN PROTEASE IN COMPLEX WITH COMPOUND 5
Zhang, C. - H., Stone, E. A., Deshmukh, M., Ippolito, J. A., Ghahremanpour, M. M., Tirado-Rives, J., Spasov, K. A., Zhang, S., Takeo, Y., Kudalkar, S. N., Liang, Z., Isaacs, F., Lindenbach, B., Miller, S. J., Anderson, K. S., and Jorgensen, W. L. (2021) Potent Noncovalent Inhibitors of the Main Protease of SARS-CoV-2 from Molecular Sculpting of the Drug Perampanel Guided by Free Energy Perturbation Calculations. ACS Cent Sci. 7, 467-475

Pages