Protein Structural Studies

Protein structural studies using Glyco-Enzymes produced using
GET recombinant protein expression technologies:

Moure, M.J., Eletsky, A., Gao, Q., Morris, L. Yang, J.Y., Chapla, D., Zhao, Y., Zong, C., Boons, G.J., Moremen, K.W., and Prestegard, J.H. (2018) Paramagnetic Tags for Glycosylation sites in Glycoproteins: Structural Constraints on Heparan Sulfate Binding

Kadirvelraj, R., Yang, J.-Y., Sanders, J.H., Liu, L., Ramiah, A., Prabhakar, P.K., Boons, G.-J., Wood, Z.A., and Moremen, K.W. (2018) Human N-acetylglucosaminyltransferase II substrate recognition uses a modular architecture that includes a convergent exosite. Proc. Natl. Acad. Sci. USA, 115:4637-4642. [PMID:29666272; PMC5939069]

Gao, Q., Yang, J.Y., Moremen, K.W., Flanagan, J.G., and Prestegard, J.H. (2018) Structural Characterization of a Heparan Sulfate Pentamer Interacting with LAR-Ig1-2. Biochemistry 57, 2189-2199. [PMID: 29570275; PMC in process]

Moremen, K.W., Ramiah, A., Stuart, M., Steel, J., Meng, L., Forouhar, F., Moniz, H.A., Gahlay, G., Gao, Z., Chapla, D., Wang, S., Yang, J.-Y., Prabahkar, P. K., Johnson, R., dela Rosa, M., Geisler, C., Nairn, A.V., Wu, S.-C., Tong, L., Gilbert, H.J., LaBaer, J., and Jarvis, D.L. (2018) Expression system for structural and functional studies of human glycosylation enzymes. Nature Chem. Biol. 14, 156-162 [PMID:29251719; PMC5774587]

Urbanowicz, B.R., Bharadwaj, V.S., Alahuhta, M., Peña, M.J., Lunin, V.V., Bomble, Y.J., Wang, S., Yang, J.-Y., Tuomivaara, S., Himmel, M.E., Moremen, K.W., York, W.S., and Crowley, M.F. (2017) Structural, Mutagenic and In Silico studies of Xyloglucan Fucosylation in Arabidopsis thaliana Suggest a Water-Mediated Mechanism. Plant J. 91: 931-949. [PMID:28670741; PMC5735850]

Gao, Q., Chalmers, G.R., Moremen, K.W., and Prestegard, J.H. (2017) NMR Assignments of Sparsely Labeled Proteins Using a Genetic Algorithm J. Biomolecular NMR. 67, 283-294. [PMID:28289927; PMC5434516]

Gao, Q., Chen, C.Y., Zong, C., Wang, S., Morris, L.C., Boons, G.-J., Moremen, K.W., and Prestegard J.H. (2016) Structural Aspects of Heparan Sulfate Binding to Robo1-D12. ACS Chemical Biology 11:3106-3113. [PMID:27653286] [PMC5148660]

Zhuo,Y., Yang, J.-Y., Moremen, K.W., and Prestegard, J. (2016) Glycosylation alters dimerization properties of a cell-surface signaling protein, CEACAM1. J. Biol. Chem. 291, 20085-95 [PMID:27471271] [PMC5025693]

Zhang, C, Zhang, T., Zou, J., Miller, C.J., Gorkhali, R., Yang, J.-Y., Schilmiller, A., Wang, S., Huang, K., Brown, E.M., Moremen, K.W., Hu, J., and Yang, J.J. (2016) Structural Basis for Regulation of Human Calcium-Sensing Receptor by Magnesium Ions and an Unexpected Tryptophan Derivative Co-agonist Science Advances, 2: e1600241 [PMID:27386547] [PMC4928972]

Li Z, Moniz HA, Wang, S., Ramiah A, Zhang, F. Moremen KW, Linhardt, R.J.,and Sharp JS (2015) High Structural Resolution Hydroxyl Radical Protein Footprinting Reveals an Extended Robo1-Heparin Binding Interface. J. Biol. Chem. 290:10729-40. [PMID 25752613] [PMC4409239]

Zhang, C., Zhuo, Y., Moniz, H.A., Wang, S., Moremen, K.W., Prestegard, J.H., Brown, E., Yang, J.J. (2014) Direct Determination of Multiple Ligand Interactions with the Extracellular Domain of the Calcium Sensing Receptor. J. Biol. Chem. 289: 33529-42 [PMID 25305020] [PMC4246106]

Prestegard, J.H., Agard, D.A., Moremen, K.W., Lavery, L.A., Morris, L.C., Pederson, K. (2014) Sparse Labeling of Proteins: Structural Characterization from Long Range Constraints. J. Mag. Res., 241, 32-40 [PMID:24656078] [PMC3964372]

Meng, L., Forouhar, F., Thieker, D., Gao, Z., Ramiah, A., Moniz, H., Xiang, Y., Seetharaman, J., Milaninia, S., Su, M., Bridger, R., Veillon, l., Azadi, P., Kornhaber, G., Wells, L., Montelione, G. T., Woods, R.J., Tong, L., and Moremen. K.W. (2013) Enzymatic basis for N-glycan sialylation: structure of rat α2,6-sialyltransferase (ST6GAL1) reveals conserved and unique features for glycan sialylation. J. Biol. Chem. 288, 34680-98 [PMID 24155237] [PMC3843080]

Barb, A.W., Meng, L., Gao, Z., Johnson, R.W., Moremen, K.W., and Prestegard, J.H. (2012) NMR Characterization of Immunoglobulin G Fc Glycan Motion on Enzymatic Sialylation. Biochemistry, 51, 4618-26. [PMID 22574931] [PMC3447994]

Liu, S., Meng, L. Moremen, K.W., and Prestegard, J.H. (2009) NMR structural characterization of substrates bound to the alpha-2,6-sialyltransferase, ST6Gal-I. Biochemistry, 48, 11211-11219 [PMID19845399] [PMC2790006]

Macnaughtan, M.A., Tian, F., Liu, S., Meng, L., Park, S., Azadi, P., Moremen, K.W., and Prestegard, J.H. (2008) 13C-Sialic Acid Labeling of Glycans on Glycoproteins Using ST6Gal-I J. Am. Chem. Soc. 130, 11864-11865 [PMID 18700760] [PMC2640832]

Barb AW, Falconer DJ, Subedi GP. (2019) The Preparation and Solution NMR Spectroscopy of Human Glycoproteins Is Accessible and Rewarding. Methods Enzymol. 614:239-261

Subedi GP, Sinitskiy AV, Roberts JT, Patel KR, Pande VS, Barb AW.(2019) Intradomain Interactions in an NMDA Receptor Fragment Mediate N-Glycan Processing and Conformational Sampling. Structure. 27:55-65

Roberts JT, Barb AW. (2018) A single amino acid distorts the Fc γ receptor IIIb/CD16b structure upon binding immunoglobulin G1 and reduces affinity relative to CD16a.J Biol Chem. 293:19899-19908.

Subedi GP, Barb AW. (2018) CD16a with oligomannose-type N-glycans is the only "low-affinity" Fc γ receptor that binds the IgG crystallizable fragment with high affinity in vitro. J Biol Chem. 293:16842-16850.

ACS Chem Biol. 2018 Aug 17;13(8):2179-2189. doi: 10.1021/acschembio.8b00342. Epub 2018 Jul 27.

Falconer DJ, Subedi GP, Marcella AM, Barb AW. (2018)Antibody Fucosylation Lowers the FcγRIIIa/CD16a Affinity by Limiting the Conformations Sampled by the N162-Glycan. ACS Chem Biol. 13:2179-2189.

Falconer DJ, Barb AW. (2018) Mouse IgG2c Fc loop residues promote greater receptor-binding affinity than mouse IgG2b or human IgG1. PLoS One. 13:e0192123.

Subedi GP, Falconer DJ, Barb AW. (2017) Carbohydrate-Polypeptide Contacts in the Antibody Receptor CD16A Identified through Solution NMR Spectroscopy. Biochemistry. 56:3174-3177.

Subedi GP, Barb AW. (2016) The immunoglobulin G1 N-glycan composition affects binding to each low affinity Fc γ receptor. MAbs. 8:1512-1524.

Subedi GP, Barb AW. (2015) The Structural Role of Antibody N-Glycosylation in Receptor Interactions. Structure. 23:1573-1583

Culbertson AT, Ehrlich JJ, Choe JY, Honzatko RB, Zabotina OA. (2018) Structure of xyloglucan xylosyltransferase 1 reveals simple steric rules that define biological patterns of xyloglucan polymers. Proc Natl Acad Sci U S A. 115:6064-6069.