You are here

Research Highlights

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

Crystal structure of SARS-CoV-2 3CL protease in complex with MAC5576

Iketani, S., Forouhar, F., Liu, H., Hong, S. Jung, Lin, F. - Y., Nair, M. S., Zask, A., Huang, Y., Xing, L., Stockwell, B. R., Chavez, A., and Ho, D. D. (2021) Lead compounds for the development of SARS-CoV-2 3CL protease inhibitors. Nat Commun. 12, 2016

Crystallographic structure of neutralizing antibody 2-51 in complex with SARS-CoV-2 spike N-terminal domain (NTD)

Cerutti, G., Guo, Y., Zhou, T., Gorman, J., Lee, M., Rapp, M., Reddem, E. R., Yu, J., Bahna, F., Bimela, J., Huang, Y., Katsamba, P. S., Liu, L., Nair, M. S., Rawi, R., Olia, A. S., Wang, P., Zhang, B., Chuang, G. - Y., Ho, D. D., Sheng, Z., Kwong, P. D., and Shapiro, L. (2021) Potent SARS-CoV-2 neutralizing antibodies directed against spike N-terminal domain target a single supersite. Cell Host Microbe. 10.1016/j.chom.2021.03.005

Crystallographic structure of neutralizing antibody 2-15 in complex with SARS-CoV-2 spike receptor-binding Domain (RBD)

Rapp, M., Guo, Y., Reddem, E. R., Yu, J., Liu, L., Wang, P., Cerutti, G., Katsamba, P., Bimela, J. S., Bahna, F. A., Mannepalli, S. M., Zhang, B., Kwong, P. D., Huang, Y., Ho, D. D., Shapiro, L., and Sheng, Z. (2021) Modular basis for potent SARS-CoV-2 neutralization by a prevalent VH1-2-derived antibody class. Cell Rep. 10.1016/j.celrep.2021.108950

Crystal structure of apo Card1

Rostøl, J. T., Xie, W., Kuryavyi, V., Maguin, P., Kao, K., Froom, R., Patel, D. J., and Marraffini, L. A. (2021) The Card1 nuclease provides defence during type III CRISPR immunity.. Nature. 590, 624-629

Tayeb-Fligelman, E., Cheng, X., Tai, C., Bowler, J. T., Griner, S., Sawaya, M. R., Seidler, P. M., Jiang, Y. Xiao, Lu, J., Rosenberg, G. M., Salwinski, L., Abskharon, R., Zee, C. - T., Hou, K., Li, Y., Boyer, D. R., Murray, K. A., Falcon, G., Anderson, D. H., Cascio, D., Saelices, L., Damoiseaux, R., Guo, F., and Eisenberg, D. S. (2021) Inhibition of amyloid formation of the Nucleoprotein of SARS-CoV-2. bioRxiv. 10.1101/2021.03.05.434000

Human SAMHD1 bound to ribo(CGCCU)-oligonucleotide

Yu, C. H., Bhattacharya, A., Persaud, M., Taylor, A. B., Wang, Z., Bulnes-Ramos, A., Xu, J., Selyutina, A., Martinez-Lopez, A., Cano, K., Demeler, B., Kim, B., Hardies, S. C., Diaz-Griffero, F., and Ivanov, D. N. (2021) Nucleic acid binding by SAMHD1 contributes to the antiretroviral activity and is enhanced by the GpsN modification. Nat Commun. 12, 731

6X9Z PDB Structure

Vorobieva, A. A., White, P., Liang, B., Horne, J. E., Bera, A. K., Chow, C. M., Gerben, S., Marx, S., Kang, A., Stiving, A. Q., Harvey, S. R., Marx, D. C., G Khan, N., Fleming, K. G., Wysocki, V. H., Brockwell, D. J., Tamm, L. K., Radford, S. E., and Baker, D. (2021) De novo design of transmembrane β barrels.. Science. 10.1126/science.abc8182

Nesprin-2G(aa1425-1649)-FHOD1(aa1-339) complex, H. sapiens

Lim, S. Mei, Cruz, V. E., Antoku, S., Gundersen, G. G., and Schwartz, T. U. (2021) Structures of FHOD1-Nesprin1/2 complexes reveal alternate binding modes for the FH3 domain of formins. Structure. 10.1016/j.str.2020.12.013

Structural basis for a germline-biased antibody response to SARS-CoV-2 (RBD:C1A-B12 Fab)

Clark, S. A., Clark, L. E., Pan, J., Coscia, A., McKay, L. G. A., Shankar, S., Johnson, R. I., Griffiths, A., and Abraham, J. (2020) Molecular basis for a germline-biased neutralizing antibody response to SARS-CoV-2. bioRxiv. 10.1101/2020.11.13.381533

6PNK Structure

Lin, L. Yingqi, McCarthy, S., Powell, B. M., Manurung, Y., Xiang, I. M., Dean, W. L., Chaires, B., and Yatsunyk, L. A. (2020) Biophysical and X-ray structural studies of the (GGGTT)3GGG G-quadruplex in complex with N-methyl mesoporphyrin IX. PLoS One. 15, e0241513

6WV3

Liu, S., Li, S., Shen, G., Sukumar, N., Krezel, A. M., and Li, W. (2020) Structural basis of antagonizing the vitamin K catalytic cycle for anticoagulation. Science. 10.1126/science.abc5667

6WX4

Rut, W., Lv, Z., Zmudzinski, M., Patchett, S., Nayak, D., Snipas, S. J., Oualid, F. El, Huang, T. T., Békés, M., Drag, M., and Olsen, S. K. (2020) Activity profiling and crystal structures of inhibitor-bound SARS-CoV-2 papain-like protease: A framework for anti-COVID-19 drug design. Sci Adv. 10.1126/sciadv.abd4596

Crystal Structure of Human Protocadherin-15 EC2-

Choudhary, D., Narui, Y., Neel, B. L., Wimalasena, L. N., Klanseck, C. F., De-la-Torre, P., Chen, C., Araya-Secchi, R., Tamilselvan, E., and Sotomayor, M. (2020) Structural determinants of protocadherin-15 mechanics and function in hearing and balance perception. Proc Natl Acad Sci U S A. 10.1073/pnas.1920444117

6W70

Polizzi, N. F., and DeGrado, W. F. (2020) A defined structural unit enables de novo design of small-molecule-binding proteins. Science. 369, 1227-1233

6WZQ

Ye, Q., West, A. M. V., Silletti, S., and Corbett, K. D. (2020) Architecture and self-assembly of the SARS-CoV-2 nucleocapsid protein. Protein Sci. 10.1002/pro.3909

M Joyce, G., Sankhala, R. S., Chen, W. - H., Choe, M., Bai, H., Hajduczki, A., Yan, L., Sterling, S. L., Peterson, C. E., Green, E. C., Smith, C., de Val, N., Amare, M., Scott, P., Laing, E. D., Broder, C. C., Rolland, M., Michael, N. L., and Modjarrad, K. (2020) A Cryptic Site of Vulnerability on the Receptor Binding Domain of the SARS-CoV-2 Spike Glycoprotein. bioRxiv. 10.1101/2020.03.15.992883

6WKS

Viswanathan, T., Arya, S., Chan, S. - H., Qi, S., Dai, N., Misra, A., Park, J. - G., Oladunni, F., Kovalskyy, D., Hromas, R. A., Martinez-Sobrido, L., and Gupta, Y. K. (2020) Structural basis of RNA cap modification by SARS-CoV-2. Nat Commun. 11, 3718

Crystal structure of the LSD1/CoREST histone demethylase bound to its nucleosome substrate

Kim, S. - A., Zhu, J., Yennawar, N., Eek, P., and Tan, S. (2020) Crystal Structure of the LSD1/CoREST Histone Demethylase Bound to Its Nucleosome Substrate. Mol Cell. 10.1016/j.molcel.2020.04.019

Structure of 2019-nCoV chimeric receptor-binding domain complexed with its receptor human ACE2

Shang, J., Ye, G., Shi, K., Wan, Y., Luo, C., Aihara, H., Geng, Q., Auerbach, A., and Li, F. (2020) Structural basis of receptor recognition by SARS-CoV-2. Nature. 10.1038/s41586-020-2179-y

Crystal Structure of the Klebsiella pneumoniae LpxH-lipid X complex

Cho, J., Lee, M., C Cochrane, S., Webster, C. G., Fenton, B. A., Zhao, J., Hong, J., and Zhou, P. (2020) Structural basis of the UDP-diacylglucosamine pyrophosphohydrolase LpxH inhibition by sulfonyl piperazine antibiotics. Proc Natl Acad Sci U S A. 117, 4109-4116

Mancia, F., and Harrison, S. C. (2020) The human dimension in contemporary biological research. Nat Struct Mol Biol. 27, 107-108

Crystal structure of ZIKV-116 Fab in complex with ZIKV envelope DIII

Zhao, H., Xu, L., Bombardi, R., Nargi, R., Deng, Z., Errico, J. M., Nelson, C. A., Dowd, K. A., Pierson, T. C., Crowe, J. E., Diamond, M. S., and Fremont, D. H. (2020) Mechanism of differential Zika and dengue virus neutralization by a public antibody lineage targeting the DIII lateral ridge. J Exp Med. 10.1084/jem.20191792

6U7B

Ye, Q., Lau, R. K., Mathews, I. T., Birkholz, E. A., Watrous, J. D., Azimi, C. S., Pogliano, J., Jain, M., and Corbett, K. D. (2019) HORMA Domain Proteins and a Trip13-like ATPase Regulate Bacterial cGAS-like Enzymes to Mediate Bacteriophage Immunity. Mol Cell. 10.1016/j.molcel.2019.12.009

Co-crystal structure of M. tuberculosis ileS T-box in complex with tRNA-3'-OH

Battaglia, R. A., Grigg, J. C., and Ke, A. (2019) Structural basis for tRNA decoding and aminoacylation sensing by T-box riboregulators. Nat Struct Mol Biol. 26, 1106-1113

6MER

Nicoludis, J. M., Green, A. G., Walujkar, S., May, E. J., Sotomayor, M., Marks, D. S., and Gaudet, R. (2019) Interaction specificity of clustered protocadherins inferred from sequence covariation and structural analysis. Proc Natl Acad Sci U S A. 116, 17825-17830

Structures of a dimodular NRPS protein reveal the central condensation state and infer very large conformational changes

Reimer, J. M., Eivaskhani, M., Harb, I., Guarné, A., Weigt, M., and T Schmeing, M. (2019) Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility. Science. 10.1126/science.aaw4388

6OON

Park, M. Seul, Araya-Secchi, R., Brackbill, J. A., Phan, H. - D., Kehling, A. C., El-Wahab, E. W. Abd, Dayeh, D. M., Sotomayor, M., and Nakanishi, K. (2019) Multidomain Convergence of Argonaute during RISC Assembly Correlates with the Formation of Internal Water Clusters. Mol Cell. 75, 725-740.e6

Structure of the full-length Clostridium difficile toxin B in complex with 3 VHHs

Chen, P., Lam, K. - H., Liu, Z., Mindlin, F. A., Chen, B., Gutierrez, C. B., Huang, L., Zhang, Y., Hamza, T., Feng, H., Matsui, T., Bowen, M. E., Perry, K., and Jin, R. (2019) Structure of the full-length Clostridium difficile toxin B. Nat Struct Mol Biol. 10.1038/s41594-019-0268-0

Crystal structure of the Protocadherin GammaB4 extracellular domain

Brasch, J., Goodman, K. M., Noble, A. J., Rapp, M., Mannepalli, S., Bahna, F., Dandey, V. P., Bepler, T., Berger, B., Maniatis, T., Potter, C. S., Carragher, B., Honig, B., and Shapiro, L. (2019) Visualization of clustered protocadherin neuronal self-recognition complexes. Nature. 569, 280-283

Crystal structure of the high-affinity copper transporter Ctr1

Ren, F., Logeman, B. L., Zhang, X., Liu, Y., Thiele, D. J., and Yuan, P. (2019) X-ray structures of the high-affinity copper transporter Ctr1. Nat Commun. 10, 1386

Structure of mouse RECON (AKR1C13) in complex with cyclic AMP-AMP-GMP (cAAG)

Whiteley, A. T., Eaglesham, J. B., Mann, C. C. de Olive, Morehouse, B. R., Lowey, B., Nieminen, E. A., Danilchanka, O., King, D. S., S Y Lee, A., Mekalanos, J. J., and Kranzusch, P. J. (2019) Bacterial cGAS-like enzymes synthesize diverse nucleotide signals. Nature. 10.1038/s41586-019-0953-5

Structure of VACV Poxin in post-reactive state with Gp[2'-5']Ap[3']

Eaglesham, J. B., Pan, Y., Kupper, T. S., and Kranzusch, P. J. (2019) Viral and metazoan poxins are cGAMP-specific nucleases that restrict cGAS-STING signalling. Nature. 566, 259-263

Pages

Quick Links

The Northeastern Collaborative Access Team (NE-CAT) facility at the Advanced Photon Source at Argonne National Laboratory is managed by Cornell University and consists of seven member institutions:

Columbia University
Cornell University
Harvard University
Memorial Sloan-Kettering Cancer Center
Massachusetts Institute of Technology
Rockefeller University
Yale University

Primary funding for this project comes from the National Institute of General Medical Sciences (NIGMS), a division of the National Institutes of Health (NIH). Additional financial support for NE-CAT comes from the member institutions.