ProfessorStephenCurry

Curry S, 2004, Plasma albumin as a fatty acid carrier, Lipobiology, Editors: Vusse, Publisher: Elsevier, Pages: 29-46, ISBN: 9780444514967

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Alfano C, Babon J, Kelly G, Curry S, Conte MRet al., 2003, Resonance assignment and secondary structure of an N-terminal fragment of the human La protein, JOURNAL OF BIOMOLECULAR NMR, Vol: 27, Pages: 93-94, ISSN: 0925-2738

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• Citations: 16

Fleming K, Ghuman J, Yuan XM, Simpson P, Szendröi A, Matthews S, Curry Set al., 2003, Solution structure and RNA interactions of the RNA recognition motif from eukaryotic translation initiation factor 4B, BIOCHEMISTRY, Vol: 42, Pages: 8966-8975, ISSN: 0006-2960

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• Citations: 22

Zunszain PA, Ghuman J, Komatsu T, Tsuchida E, Curry Set al., 2003, Crystal structural analysis of human serum albumin complexed with hemin and fatty acid., BMC Struct Biol, Vol: 3

BACKGROUND: Human serum albumin (HSA) is an abundant plasma protein that binds a wide variety of hydrophobic ligands including fatty acids, bilirubin, thyroxine and hemin. Although HSA-heme complexes do not bind oxygen reversibly, it may be possible to develop modified HSA proteins or heme groups that will confer this ability on the complex. RESULTS: We present here the crystal structure of a ternary HSA-hemin-myristate complex, formed at a 1:1:4 molar ratio, that contains a single hemin group bound to subdomain IB and myristate bound at six sites. The complex displays a conformation that is intermediate between defatted HSA and HSA-fatty acid complexes; this is likely to be due to low myristate occupancy in the fatty acid binding sites that drive the conformational change. The hemin group is bound within a narrow D-shaped hydrophobic cavity which usually accommodates fatty acid; the hemin propionate groups are coordinated by a triad of basic residues at the pocket entrance. The iron atom in the centre of the hemin is coordinated by Tyr161. CONCLUSION: The structure of the HSA-hemin-myristate complex (PDB ID 1o9x) reveals the key polar and hydrophobic interactions that determine the hemin-binding specificity of HSA. The details of the hemin-binding environment of HSA provide a structural foundation for efforts to modify the protein and/or the heme molecule in order to engineer complexes that have favourable oxygen-binding properties.

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Jacks A, Babon J, Kelly G, Manolaridis I, Cary PD, Curry S, Conte MRet al., 2003, Structure of the C-terminal domain of human La protein reveals a novel RNA recognition motif coupled to a helical nuclear retention element, STRUCTURE, Vol: 11, Pages: 833-843, ISSN: 0969-2126

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• Citations: 89

Petitpas I, Petersen CE, Ha CE, Bhattacharya AA, Zunszain PA, Ghuman J, Bhagavan NV, Curry Set al., 2003, Structural basis of albumin-thyroxine interactions and familial dysalbuminemic hyperthyroxinemia, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, Vol: 100, Pages: 6440-6445, ISSN: 0027-8424

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• Citations: 195

Iyer LM, Koonin EV, Aravind L, 2003, Evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases and the origin of RNA polymerases., BMC Struct Biol, Vol: 3

BACKGROUND: The eukaryotic RNA-dependent RNA polymerase (RDRP) is involved in the amplification of regulatory microRNAs during post-transcriptional gene silencing. This enzyme is highly conserved in most eukaryotes but is missing in archaea and bacteria. No evolutionary relationship between RDRP and other polymerases has been reported so far, hence the origin of this eukaryote-specific polymerase remains a mystery. RESULTS: Using extensive sequence profile searches, we identified bacteriophage homologs of the eukaryotic RDRP. The comparison of the eukaryotic RDRP and their homologs from bacteriophages led to the delineation of the conserved portion of these enzymes, which is predicted to harbor the catalytic site. Further, detailed sequence comparison, aided by examination of the crystal structure of the DNA-dependent RNA polymerase (DDRP), showed that the RDRP and the beta' subunit of DDRP (and its orthologs in archaea and eukaryotes) contain a conserved double-psi beta-barrel (DPBB) domain. This DPBB domain contains the signature motif DbDGD (b is a bulky residue), which is conserved in all RDRPs and DDRPs and contributes to catalysis via a coordinated divalent cation. Apart from the DPBB domain, no similarity was detected between RDRP and DDRP, which leaves open two scenarios for the origin of RDRP: i) RDRP evolved at the onset of the evolution of eukaryotes via a duplication of the DDRP beta' subunit followed by dramatic divergence that obliterated the sequence similarity outside the core catalytic domain and ii) the primordial RDRP, which consisted primarily of the DPBB domain, evolved from a common ancestor with the DDRP at a very early stage of evolution, during the RNA world era. The latter hypothesis implies that RDRP had been subsequently eliminated from cellular life forms and might have been reintroduced into the eukaryotic genomes through a bacteriophage. Sequence and structure analysis of the DDRP led to further insights into the evolution of RNA polym

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Simpson PJ, Davydova N, Curry S, Matthews Set al., 2002, Letter to the Editor:: Resonance assignment and topology of the <SUP>2</SUP>H, <SUP>13</SUP>C, <SUP>15</SUP>N labelled 29 kDa N-terminal fragment of the polypyrimidine tract binding protein (PTB), JOURNAL OF BIOMOLECULAR NMR, Vol: 24, Pages: 79-80, ISSN: 0925-2738

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• Citations: 3

Simpson PJ, Davydova N, Curry S, Matthews Set al., 2002, Resonance assignment and topology of the 2H, 13C, 15N labelled 29 kDa N-terminal fragment of the polypyrimidine tract binding protein (PTB)., J Biomol NMR, Vol: 24, Pages: 79-80, ISSN: 0925-2738

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Curry S, 2002, Beyond expansion: Structural studies on the transport roles of human serum albumin, VOX SANGUINIS, Vol: 83, Pages: 315-319, ISSN: 0042-9007

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• Citations: 91

Choi JK, Ho J, Curry S, Qin DH, Bittman R, Hamilton JAet al., 2002, Interactions of very long-chain saturated fatty acids with serum albumin, JOURNAL OF LIPID RESEARCH, Vol: 43, Pages: 1000-1010, ISSN: 0022-2275

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• Citations: 97

Petersen CE, Ha CE, Curry S, Bhagavan NVet al., 2002, Probing the structure of the warfarin-binding site on human serum albumin using site-directed mutagenesis, PROTEINS-STRUCTURE FUNCTION AND GENETICS, Vol: 47, Pages: 116-125, ISSN: 0887-3585

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• Citations: 42

Jacks A, Kelly G, Curry S, Conte MRet al., 2002, Letter to the Editor: Resonance assignment and secondary structure determination of a C-terminal fragment of the Lupus Autoantigen (La) protein containing a putative RNA recognition motif (RRM), JOURNAL OF BIOMOLECULAR NMR, Vol: 22, Pages: 387-388, ISSN: 0925-2738

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• Citations: 4

Yuan XM, Davydova N, Conte MR, Curry S, Matthews Set al., 2002, Chemical shift mapping of RNA interactions with the polypyrimidine tract binding protein, NUCLEIC ACIDS RESEARCH, Vol: 30, Pages: 456-462, ISSN: 0305-1048

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• Citations: 25

Ghuman J, Petitpas I, Bhattacharya A, Curry Set al., 2002, CRYSTALLOGRAPHIC STUDIES OF SITE I DRUGS BOUND TO THE HUMAN SERUM ALBUMIN-MYRISTATE COMPLEX, Publisher: INT UNION CRYSTALLOGRAPHY, Pages: C232-C232, ISSN: 2053-2733

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Petitpas I, Grüne T, Bhattacharya AA, Curry Set al., 2001, Crystal structures of human serum albumin complexed with monounsaturated and polyunsaturated fatty acids, JOURNAL OF MOLECULAR BIOLOGY, Vol: 314, Pages: 955-960, ISSN: 0022-2836

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• Citations: 399

Petitpas I, Bhattacharya AA, Twine S, East M, Curry Set al., 2001, Crystal structure analysis of warfarin binding to human serum albumin - Anatomy of drug site I, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 276, Pages: 22804-22809, ISSN: 0021-9258

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• Citations: 691

Bhattacharya AA, Curry S, Franks NP, 2000, Binding of the general anesthetics propofol and halothane to human serum albumin - High resolution crystal structures, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 275, Pages: 38731-38738, ISSN: 0021-9258

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• Citations: 480

Bhattacharya AA, Grüne T, Curry S, 2000, Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin, JOURNAL OF MOLECULAR BIOLOGY, Vol: 303, Pages: 721-732, ISSN: 0022-2836

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• Citations: 737

Conte MR, Grüne T, Ghuman J, Kelly G, Ladas A, Matthews S, Curry Set al., 2000, Structure of tandem RNA recognition motifs from polypyrimidine tract binding protein reveals novel features of the RRM fold, EMBO JOURNAL, Vol: 19, Pages: 3132-3141, ISSN: 0261-4189

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• Citations: 128

Belnap DM, Filman DJ, Trus BL, Cheng NQ, Booy FP, Conway JF, Curry S, Hiremath CN, Tsang SK, Steven AC, Hogle JMet al., 2000, Molecular tectonic model of virus structural transitions: the putative cell entry states of poliovirus, JOURNAL OF VIROLOGY, Vol: 74, Pages: 1342-1354, ISSN: 0022-538X

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• Citations: 195

Curry S, Brick P, Franks NP, 1999, Fatty acid binding to human serum albumin: new insights from crystallographic studies, BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS, Vol: 1441, Pages: 131-140, ISSN: 1388-1981

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• Citations: 444

Conte MR, Grüne T, Curry S, Matthews Set al., 1999, Resonance assignment and topology of a 22 kDa C-terminal fragment of the polypyrimidine tract binding protein (PTB) containing two RNA binding domains, JOURNAL OF BIOMOLECULAR NMR, Vol: 14, Pages: 383-384, ISSN: 0925-2738

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• Citations: 2

Belnap D, Filman D, Trus B, Booy F, Cheng N, Curry S, Hiremath C, Tsang S, Hogle J, Steven Aet al., 1999, Springing the trap: Conformational changes when poliovirus switches into cell-entry intermediate and RNA-released states, BIOPHYSICAL JOURNAL, Vol: 76, Pages: A27-A27, ISSN: 0006-3495

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Bhattacharya A, Grune T, Franks NP, Curry Set al., 1999, CRYSTALLOGRAPHIC ANALYSIS OF DRUG INTERACTIONS WITH HUMAN SERUM ALBUMIN., Publisher: INT UNION CRYSTALLOGRAPHY, Pages: 366-366, ISSN: 2053-2733

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Curry S, Mandelkow H, Brick P, Franks Net al., 1998, Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites, NATURE STRUCTURAL BIOLOGY, Vol: 5, Pages: 827-835, ISSN: 1072-8368

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• Citations: 1165

van Vlijmen HWT, Curry S, Schaefer M, Karplus Met al., 1998, Titration calculations of foot-and-mouth disease virus capsids and their stabilities as a function of pH, JOURNAL OF MOLECULAR BIOLOGY, Vol: 275, Pages: 295-308, ISSN: 0022-2836

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• Citations: 55

Curry S, Fry E, Blakemore W, AbuGhazaleh R, Jackson T, King A, Lea S, Newman J, Stuart Det al., 1997, Dissecting the roles of VP0 cleavage and RNA packaging in picornavirus capsid stabilization: The structure of empty capsids of foot-and-mouth disease virus, JOURNAL OF VIROLOGY, Vol: 71, Pages: 9743-9752, ISSN: 0022-538X

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• Citations: 120

Wien MW, Curry S, Filman DJ, Hogle JMet al., 1997, Structural studies of poliovirus mutants that overcome receptor defects, NATURE STRUCTURAL BIOLOGY, Vol: 4, Pages: 666-674, ISSN: 1072-8368

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• Citations: 39

Curry S, Chow M, Hogle JM, 1996, The poliovirus 135S particle is infectious, JOURNAL OF VIROLOGY, Vol: 70, Pages: 7125-7131, ISSN: 0022-538X

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• Citations: 109