Publications
131 results found
Leen EN, Kwok KYR, Birtley JR, et al., 2013, Structures of the Compact Helical Core Domains of Feline Calicivirus and Murine Norovirus VPg Proteins, JOURNAL OF VIROLOGY, Vol: 87, Pages: 5318-5330, ISSN: 0022-538X
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- Citations: 36
Curry S, 2013, Open access: brave new world requires bravery, Insights, Vol: 26, Pages: 22-27, ISSN: 2048-7754
Porta C, Xu X, Loureiro S, et al., 2013, Efficient production of foot-and-mouth disease virus empty capsids in insect cells following down regulation of 3C protease activity, JOURNAL OF VIROLOGICAL METHODS, Vol: 187, Pages: 406-412, ISSN: 0166-0934
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- Citations: 42
Kafasla P, Mickleburgh I, Llorian M, et al., 2012, Defining the roles and interactions of PTB, BIOCHEMICAL SOCIETY TRANSACTIONS, Vol: 40, Pages: 815-820, ISSN: 0300-5127
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- Citations: 61
Curry S, 2012, Access all areas, NEW SCIENTIST, Vol: 214, Pages: 26-27, ISSN: 0262-4079
Curry S, 2012, Access all areas, NEW SCIENTIST, Vol: 214, Pages: 26-27, ISSN: 0262-4079
Leen EN, Baeza G, Curry S, 2012, Structure of a Murine Norovirus NS6 Protease-Product Complex Revealed by Adventitious Crystallisation, PLOS ONE, Vol: 7, ISSN: 1932-6203
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- Citations: 20
Curry S, 2012, By the people, for the people, New Scientist, Vol: 214, Pages: 26-27, ISSN: 0262-4079
Martino L, Pennell S, Kelly G, et al., 2012, Analysis of the interaction with the hepatitis C virus mRNA reveals an alternative mode of RNA recognition by the human La protein, NUCLEIC ACIDS RESEARCH, Vol: 40, Pages: 1381-1394, ISSN: 0305-1048
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- Citations: 41
Joshi A, Coelho MB, Kotik-Kogan O, et al., 2011, Crystallographic analysis of polypyrimidine tract-binding protein-Raver1 interactions involved in regulation of alternative splicing., Structure, Vol: 19, Pages: 1816-1825
The polypyrimidine tract-binding protein (PTB) is an important regulator of alternative splicing. PTB-regulated splicing of α-tropomyosin is enhanced by Raver1, a protein with four PTB-Raver1 interacting motifs (PRIs) that bind to the helical face of the second RNA recognition motif (RRM2) in PTB. We present the crystal structures of RRM2 in complex with PRI3 and PRI4 from Raver1, which--along with structure-based mutagenesis--reveal the molecular basis of their differential binding. High-affinity binding by Raver1 PRI3 involves shape-matched apolar contacts complemented by specific hydrogen bonds, a new variant of an established mode of peptide-RRM interaction. Our results refine the sequence of the PRI motif and place important structural constraints on functional models of PTB-Raver1 interactions. Our analysis indicates that the observed Raver1-PTB interaction is a general mode of binding that applies to Raver1 complexes with PTB paralogues such as nPTB and to complexes of Raver2 with PTB.
Jamal SM, Ferrari G, Ahmed S, et al., 2011, Evolutionary analysis of serotype A foot-and-mouth disease viruses circulating in Pakistan and Afghanistan during 2002-2009, JOURNAL OF GENERAL VIROLOGY, Vol: 92, Pages: 2849-2864, ISSN: 0022-1317
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- Citations: 43
Kafasla P, Lin H, Curry S, et al., 2011, Activation of picornaviral IRESs by PTB shows differential dependence on each PTB RNA-binding domain, RNA, Vol: 17, Pages: 1120-1131, ISSN: 1355-8382
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- Citations: 26
Nishi K, Ono T, Nakamura T, et al., 2011, Structural Insights into Differences in Drug-binding Selectivity between Two Forms of Human α1-Acid Glycoprotein Genetic Variants, the A and F1*S Forms, Journal of Biological Chemistry, Vol: 286, Pages: 14427-14434, ISSN: 1083-351X
Human α(1)-acid glycoprotein (hAGP) in serum functions as a carrier of basic drugs. In most individuals, hAGP exists as a mixture of two genetic variants, the F1*S and A variants, which bind drugs with different selectivities. We prepared a mutant of the A variant, C149R, and showed that its drug-binding properties were indistinguishable from those of the wild type. In this study, we determined the crystal structures of this mutant hAGP alone and complexed with disopyramide (DSP), amitriptyline (AMT), and the nonspecific drug chlorpromazine (CPZ). The crystal structures revealed that the drug-binding pocket on the A variant is located within an eight-stranded β-barrel, similar to that found in the F1*S variant and other lipocalin family proteins. However, the binding region of the A variant is narrower than that of the F1*S variant. In the crystal structures of complexes with DSP and AMT, the two aromatic rings of each drug interact with Phe-49 and Phe-112 at the bottom of the binding pocket. Although the structure of CPZ is similar to those of DSP and AMT, its fused aromatic ring system, which is extended in length by the addition of a chlorine atom, appears to dictate an alternative mode of binding, which explains its nonselective binding to the F1*S and A variant hAGPs. Modeling experiments based on the co-crystal structures suggest that, in complexes of DSP, AMT, or CPZ with the F1*S variant, Phe-114 sterically hinders interactions with DSP and AMT, but not CPZ.
Ryan AJ, Chung C-W, Curry S, 2011, Crystallographic analysis reveals the structural basis of the high-affinity binding of iophenoxic acid to human serum albumin, BMC STRUCTURAL BIOLOGY, Vol: 11
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- Citations: 30
Ryan AJ, Ghuman J, Zunszain PA, et al., 2010, Structural basis of binding of fluorescent, site-specific dansylated amino acids to human serum albumin, Journal of Structural Biology, Vol: 174, Pages: 84-91, ISSN: 1095-8657
Sweeney TR, Cisnetto V, Bose D, et al., 2010, Foot-and-Mouth Disease Virus 2C Is a Hexameric AAA plus Protein with a Coordinated ATP Hydrolysis Mechanism, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 285, Pages: 24347-24359
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- Citations: 50
Klopfleisch C, Minh LQ, Giesow K, et al., 2010, Effect of foot-and-mouth disease virus capsid precursor protein and 3C protease expression on bovine herpesvirus 1 replication, ARCHIVES OF VIROLOGY, Vol: 155, Pages: 723-731, ISSN: 0304-8608
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- Citations: 4
Zunszain PA, Knox SR, Sweeney TR, et al., 2010, Insights into Cleavage Specificity from the Crystal Structure of Foot-and-Mouth Disease Virus 3C Protease Complexed with a Peptide Substrate, JOURNAL OF MOLECULAR BIOLOGY, Vol: 395, Pages: 375-389, ISSN: 0022-2836
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- Citations: 53
Curry S, 2010, More light and colour. Science and the new media, Biochemist, Vol: 32, Pages: 18-21, ISSN: 0954-982X
Liu Y, Garnett JA, Leon E, et al., 2009, Detailed insights from microarray and crystallographic studies into carbohydrate recognition by microneme protein 1 (MIC1) of Toxoplasma gondii, Protein Sci., Vol: 18, Pages: 1935-1947
The intracellular protozoan Toxoplasma gondii is among the most widespread parasites. The broad host cell range of the parasite can be explained by carbohydrate microarray screening analyses that have demonstrated the ability of the T. gondii adhesive protein, TgMIC1, to bind to a wide spectrum of sialyl oligosaccharide ligands. Here, we investigate by further microarray analyses in a dose-response format the differential binding of TgMIC1 to 2-3- and 2-6-linked sialyl carbohydrates. Interestingly, two novel synthetic fluorinated analogs of 3'SiaLacNAc(1-4) and 3'SiaLacNAc(1-3) were identified as highly potent ligands. To understand the structural basis of the carbohydrate binding specificity of TgMIC1, we have determined the crystal structures of TgMIC1 micronemal adhesive repeat (MAR)-region (TgMIC1-MARR) in complex with five sialyl-N-acetyllactosamine analogs. These crystal structures have revealed a specific, water-mediated hydrogen bond network that accounts for the preferential binding of TgMIC1-MARR to arrayed 2-3-linked sialyl oligosaccharides and the high potency of the fluorinated analogs. Furthermore, we provide strong evidence for the first observation of a C--F...H--O hydrogen bond within a lectin-carbohydrate complex. Finally, detailed comparison with other oligosaccharide-protein complexes in the Protein Data Bank (PDB) reveals a new family of sialic-acid binding sites from lectins in parasites, bacteria, and viruses
Nakagawa A, Komatsu T, Curry S, et al., 2009, O<sub>2</sub> Binding Properties of Human Serum Albumin Quadruple Mutant Complexed Iron Protoporphyrin IX with Axial His-186 Coordination, CHEMISTRY LETTERS, Vol: 38, Pages: 776-777, ISSN: 0366-7022
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- Citations: 1
Curry S, Kotik-Kogan O, Conte MR, et al., 2009, Getting to the end of RNA: Structural analysis of protein recognition of 5′ and 3′ termini, BIOCHIMICA ET BIOPHYSICA ACTA-GENE REGULATORY MECHANISMS, Vol: 1789, Pages: 653-666, ISSN: 1874-9399
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- Citations: 19
Kafasla P, Morgner N, Poeyry TAA, et al., 2009, Polypyrimidine Tract Binding Protein Stabilizes the Encephalomyocarditis Virus IRES Structure via Binding Multiple Sites in a Unique Orientation, MOLECULAR CELL, Vol: 34, Pages: 556-568, ISSN: 1097-2765
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- Citations: 72
Curry S, 2009, Widen the channels of communication with society, NATURE, Vol: 458, Pages: 702-703, ISSN: 0028-0836
Curry S, 2009, Journal club. A crystallographer takes a jaunt into immunology., Nature, Vol: 457
Komatsu T, Nakagawa A, Curry S, et al., 2009, The role of an amino acid triad at the entrance of the heme pocket in human serum albumin for O<sub>2</sub> and CO binding to iron protoporphyrin IX, ORGANIC & BIOMOLECULAR CHEMISTRY, Vol: 7, Pages: 3836-3841, ISSN: 1477-0520
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- Citations: 12
Curry S, 2009, Lessons from the Crystallographic Analysis of Small Molecule Binding to Human Serum Albumin, DRUG METABOLISM AND PHARMACOKINETICS, Vol: 24, Pages: 342-357, ISSN: 1347-4367
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- Citations: 229
Sanfelice D, Kelly G, Curry S, et al., 2008, NMR assignment of the N-terminal region of human La free and in complex with RNA, BIOMOLECULAR NMR ASSIGNMENTS, Vol: 2, Pages: 107-109, ISSN: 1874-2718
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- Citations: 10
Zunszain PA, Ghuman J, McDonagh AF, et al., 2008, Crystallographic analysis of human serum albumin complexed with 4<i>Z</i>,15<i>E</i>-bilirubin-IXα, JOURNAL OF MOLECULAR BIOLOGY, Vol: 381, Pages: 394-406, ISSN: 0022-2836
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- Citations: 221
Kotik-Kogan O, Valentine ER, Sanfelice D, et al., 2008, Structural analysis reveals conformational plasticity in the recognition of RNA 3′ ends by the human La protein, STRUCTURE, Vol: 16, Pages: 852-862, ISSN: 0969-2126
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- Citations: 62
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