L N Johnson

Summary

Affiliation: University of Oxford
Country: UK

Publications

  1. ncbi request reprint Structural studies with inhibitors of the cell cycle regulatory kinase cyclin-dependent protein kinase 2
    Louise N Johnson
    Laboratory of Molecular Biophysics, Department of Biochemistry, University of Oxford, Rex Richards Building, South Parks Road, OX1 3QU, Oxford, UK
    Pharmacol Ther 93:113-24. 2002
  2. ncbi request reprint The Eleventh Datta Lecture. The structural basis for substrate recognition and control by protein kinases
    L N Johnson
    Laboratory of Molecular Biophysics and Oxford Centre for Molecular Sciences, University of Oxford, UK
    FEBS Lett 430:1-11. 1998
  3. ncbi request reprint Control by phosphorylation
    L N Johnson
    Laboratory of Molecular Biophysics, University of Oxford, UK
    Curr Opin Struct Biol 6:762-9. 1996
  4. ncbi request reprint Structural studies on phospho-CDK2/cyclin A bound to nitrate, a transition state analogue: implications for the protein kinase mechanism
    A Cook
    Laboratory of Molecular Biophysics, Department of Biochemistry, University of Oxford, Rex Richards Building, South Parks Road, Oxford OX1 3QU, U K
    Biochemistry 41:7301-11. 2002
  5. ncbi request reprint The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases
    N R Brown
    Laboratory of Molecular Biophysics and Oxford Centre for Molecular Sciences, Department of Biochemistry, University of Oxford, Rex Richards Building, South Parks Road, Oxford OX1 3QU, UK
    Nat Cell Biol 1:438-43. 1999
  6. ncbi request reprint Effects of phosphorylation of threonine 160 on cyclin-dependent kinase 2 structure and activity
    N R Brown
    Laboratory of Molecular Biophysics, Department of Biochemistry, and Oxford Centre for Molecular Sciences, University of Oxford, The Rex Richards Building, South Parks Road, Oxford OX1 3QU, United Kingdom
    J Biol Chem 274:8746-56. 1999
  7. ncbi request reprint The crystal structure of the Escherichia coli maltodextrin phosphorylase-acarbose complex
    M O'REILLY
    Laboratory of Molecular Biophysics, Oxford Centre for Molecular Sciences, Department of Biochemistry, University of Oxford, U K
    Biochemistry 38:5337-45. 1999
  8. ncbi request reprint Pyridoxal phosphate site in glycogen phosphorylase b: structure in native enzyme and in three derivatives with modified cofactors
    N G Oikonomakos
    Laboratory of Molecular Biophysics, University of Oxford, U K
    Biochemistry 26:8381-9. 1987
  9. ncbi request reprint Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2
    H Song
    Department of Biochemistry, University of Oxford, United Kingdom
    Mol Cell 7:615-26. 2001
  10. ncbi request reprint Refined crystal structure of the phosphorylase-heptulose 2-phosphate-oligosaccharide-AMP complex
    L N Johnson
    Laboratory of Molecular Biophysics, Oxford, U K
    J Mol Biol 211:645-61. 1990

Collaborators

Detail Information

Publications28

  1. ncbi request reprint Structural studies with inhibitors of the cell cycle regulatory kinase cyclin-dependent protein kinase 2
    Louise N Johnson
    Laboratory of Molecular Biophysics, Department of Biochemistry, University of Oxford, Rex Richards Building, South Parks Road, OX1 3QU, Oxford, UK
    Pharmacol Ther 93:113-24. 2002
    ..We describe the structure of phospho-CDK2 in complex with kinase-associated phosphatase, and discuss the substrate recognition promoted by interactions that are remote from the catalytic site...
  2. ncbi request reprint The Eleventh Datta Lecture. The structural basis for substrate recognition and control by protein kinases
    L N Johnson
    Laboratory of Molecular Biophysics and Oxford Centre for Molecular Sciences, University of Oxford, UK
    FEBS Lett 430:1-11. 1998
    ....
  3. ncbi request reprint Control by phosphorylation
    L N Johnson
    Laboratory of Molecular Biophysics, University of Oxford, UK
    Curr Opin Struct Biol 6:762-9. 1996
    ..The new results highlight the importance of the phosphoamino acids both in the organization of local regions of protein structure through phosphate-arginine interactions and in the promotion of long-range conformational responses...
  4. ncbi request reprint Structural studies on phospho-CDK2/cyclin A bound to nitrate, a transition state analogue: implications for the protein kinase mechanism
    A Cook
    Laboratory of Molecular Biophysics, Department of Biochemistry, University of Oxford, Rex Richards Building, South Parks Road, Oxford OX1 3QU, U K
    Biochemistry 41:7301-11. 2002
    ....
  5. ncbi request reprint The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases
    N R Brown
    Laboratory of Molecular Biophysics and Oxford Centre for Molecular Sciences, Department of Biochemistry, University of Oxford, Rex Richards Building, South Parks Road, Oxford OX1 3QU, UK
    Nat Cell Biol 1:438-43. 1999
    ..These residues include the RXL motif required to target p107 to cyclins. This structure explains the specificity of the RXL motif for cyclins...
  6. ncbi request reprint Effects of phosphorylation of threonine 160 on cyclin-dependent kinase 2 structure and activity
    N R Brown
    Laboratory of Molecular Biophysics, Department of Biochemistry, and Oxford Centre for Molecular Sciences, University of Oxford, The Rex Richards Building, South Parks Road, Oxford OX1 3QU, United Kingdom
    J Biol Chem 274:8746-56. 1999
    ..The majority of these states are likely to correspond to inactive conformations, but a small fraction of phosphorylated CDK2 may be in an active conformation and hence explain the basal activity observed...
  7. ncbi request reprint The crystal structure of the Escherichia coli maltodextrin phosphorylase-acarbose complex
    M O'REILLY
    Laboratory of Molecular Biophysics, Oxford Centre for Molecular Sciences, Department of Biochemistry, University of Oxford, U K
    Biochemistry 38:5337-45. 1999
    ..This flexibility allows acarbose to target a number of different enzymes. The two alternative conformations of acarbose when bound to different carbohydrate enzymes are discussed...
  8. ncbi request reprint Pyridoxal phosphate site in glycogen phosphorylase b: structure in native enzyme and in three derivatives with modified cofactors
    N G Oikonomakos
    Laboratory of Molecular Biophysics, University of Oxford, U K
    Biochemistry 26:8381-9. 1987
    ..abstract truncated at 250 words)..
  9. ncbi request reprint Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2
    H Song
    Department of Biochemistry, University of Oxford, United Kingdom
    Mol Cell 7:615-26. 2001
    ..This interaction requires that the activation segment is unfolded and drawn away from the kinase molecule, inducing a conformation of CDK2 similar to the activated state observed in the CDK2/cyclin A complex...
  10. ncbi request reprint Refined crystal structure of the phosphorylase-heptulose 2-phosphate-oligosaccharide-AMP complex
    L N Johnson
    Laboratory of Molecular Biophysics, Oxford, U K
    J Mol Biol 211:645-61. 1990
    ..In both reactions the substrate phosphate plays a key role in transition state stabilization. The details of the oligosaccharide, maltoheptaose, interactions with the enzyme at the glycogen storage site are also described...
  11. ncbi request reprint Structural mechanism for glycogen phosphorylase control by phosphorylation and AMP
    D Barford
    Laboratory of Molecular Biophysics, University of Oxford, U K
    J Mol Biol 218:233-60. 1991
    ..abstract truncated at 400 words)..
  12. ncbi request reprint Xenopus phospho-CDK7/cyclin H expressed in baculoviral-infected insect cells
    A M Lawrie
    Laboratory of Molecular Biophysics and Oxford Centre for Molecular Sciences, Biochemistry Department, University of Oxford, Rex Richards Building, South Parks Road, Oxford OX1 3QU, United Kingdom
    Protein Expr Purif 23:252-60. 2001
    ..We discuss the occurrence of in vivo phosphorylation of proteins expressed in baculoviral-infected insect cells...
  13. pmc The structure of a glycogen phosphorylase glucopyranose spirohydantoin complex at 1.8 A resolution and 100 K: the role of the water structure and its contribution to binding
    M Gregoriou
    Laboratory of Molecular Biophysics and Oxford Centre for Molecular Sciences, University of Oxford, United Kingdom
    Protein Sci 7:915-27. 1998
    ..The ability of the inhibitor to exploit existing waters, to displace waters and to recruit new waters appears to be important for the high affinity of the inhibitor...
  14. ncbi request reprint Channels at the catalytic site of glycogen phosphorylase b: binding and kinetic studies with the beta-glycosidase inhibitor D-gluconohydroximo-1,5-lactone N-phenylurethane
    D Barford
    Laboratory of Molecular Biophysics, University of Oxford, U K
    Biochemistry 27:6733-41. 1988
    ..The glucopyranosylidene ring, in the half-chair conformation, occupies a similar but not identical position (shift about 0.6 A) to that occupied by other glucosyl compounds bound at the catalytic site.(ABSTRACT TRUNCATED AT 250 WORDS)..
  15. ncbi request reprint Comparison of the binding of glucose and glucose 1-phosphate derivatives to T-state glycogen phosphorylase b
    J L Martin
    Laboratory of Molecular Biophysics, Oxford, U K
    Biochemistry 29:10745-57. 1990
    ..The conformation of this stretch of residues is different from that observed in glycogen phosphorylase a...
  16. pmc The crystal structure of Escherichia coli maltodextrin phosphorylase provides an explanation for the activity without control in this basic archetype of a phosphorylase
    K A Watson
    Laboratory of Molecular Biophysics, Oxford, UK
    EMBO J 16:1-14. 1997
    ..The open access to the conserved catalytic site provides an explanation for the activity without control in this basic archetype of a phosphorylase...
  17. ncbi request reprint Oligosaccharide substrate binding in Escherichia coli maltodextrin phosphorylase
    M O'REILLY
    Laboratory of Molecular Biophysics, University of Oxford
    Nat Struct Biol 4:405-12. 1997
    ....
  18. pmc The crystal structure of a phosphorylase kinase peptide substrate complex: kinase substrate recognition
    E D Lowe
    Laboratory of Molecular Biophysics and Oxford Centre for Molecular Sciences, University of Oxford, Rex Richards Building, South Parks Road, Oxford OX1 3QU, UK
    EMBO J 16:6646-58. 1997
    ..The catalytic core of PHK exists as a dimer in crystals of the ternary complex, and the relevance of this phenomenon to its in vivo recognition of dimeric glycogen phosphorylase b is considered...
  19. ncbi request reprint The crystal structure of cyclin A
    N R Brown
    Laboratory of Molecular Biophysics, Oxford, UK
    Structure 3:1235-47. 1995
    ..From the determination of the structure of cyclin A, together with results from biochemical and genetic analyses, we can identify which parts of the cyclin molecular may contribute to cyclin A structure and function...
  20. pmc Phosphorylase recognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question
    K A Watson
    Laboratory of Molecular Biophysics, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK
    EMBO J 18:4619-32. 1999
    ..In all three complexes the pentasaccharide exhibits an altered conformation across sub-sites -1 and +1, the site of catalysis, from the preferred conformation for alpha(1-4)-linked glucosyl polymers...
  21. pmc Laue and monochromatic diffraction studies on catalysis in phosphorylase b crystals
    E M Duke
    Laboratory of Molecular Biophysics, University of Oxford, United Kingdom
    Protein Sci 3:1178-96. 1994
    ..abstract truncated at 250 words)..
  22. ncbi request reprint Glucose analogue inhibitors of glycogen phosphorylase: the design of potential drugs for diabetes
    J L Martin
    Laboratory of Molecular Biophysics, Oxford, U K
    Biochemistry 30:10101-16. 1991
    ..The beta pocket was shown to bind gentiobiose (6-O-beta-D-glucopyranosyl-D-glucose), indicating scope for binding of larger side groups for future studies...
  23. ncbi request reprint Two structures of the catalytic domain of phosphorylase kinase: an active protein kinase complexed with substrate analogue and product
    D J Owen
    Laboratory of Molecular Biophysics, University of Oxford, UK
    Structure 3:467-82. 1995
    ..Structural studies of phosphorylase kinase (Phk), the major substrate of which is glycogen phosphorylase, may be expected to shed light on its regulation...
  24. ncbi request reprint Structure of human transthyretin complexed with bromophenols: a new mode of binding
    M Ghosh
    Laboratory of Molecular Biophysics, Department of Biochemistry, South Parks Road, Oxford OX1 3QU, England
    Acta Crystallogr D Biol Crystallogr 56:1085-95. 2000
    ..The interactions with the halogens are smaller in number in TTR-TBP and there is a decrease in affinity, even though the interaction with the hydroxyl group is stronger than that in the TTR-PBP complex...
  25. ncbi request reprint Glycogen phosphorylase: control by phosphorylation and allosteric effectors
    L N Johnson
    Laboratory of Molecular Biophysics, University of Oxford, England
    FASEB J 6:2274-82. 1992
    ..The allosteric mechanism of activation of phosphorylase by phosphorylation may be relevant to other enzymes although it is now known that other mechanisms such as electrostatic steric blocking mechanisms also exist...
  26. ncbi request reprint Protein kinase inhibition by staurosporine revealed in details of the molecular interaction with CDK2
    A M Lawrie
    Nat Struct Biol 4:796-801. 1997
    ..The structure of a CDK2 staurosporine complex explains the tight binding of this inhibitor, and suggests features to be exploited in the design of specific inhibitors of CDKs...
  27. ncbi request reprint Enzymatic catalysis in crystals of Escherichia coli maltodextrin phosphorylase
    S Geremia
    CEB Centre of Excellence in Biocrystallography, Department of Chemical Sciences, University of Trieste, Via L Giorgieri 1, 34127 Trieste, Italy
    J Mol Biol 322:413-23. 2002
    ..This movie reveals the relative positions of substrates in the catalytic channel and shows a minimal movement of the protein, involving mainly Arg569, which tracks the substrate phosphate group...
  28. ncbi request reprint Follistatin: essential role for the N-terminal domain in activin binding and neutralization
    Y Sidis
    Reproductive Endocrine Unit and National Center for Infertility Research and the Endocrine Unit, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts 02114, USA
    J Biol Chem 276:17718-26. 2001
    ....