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  1. Article

    Open Access

    Esperanto for histones: CENP-A, not CenH3, is the centromeric histone H3 variant

    The first centromeric protein identified in any species was CENP-A, a divergent member of the histone H3 family that was recognised by autoantibodies from patients with scleroderma-spectrum disease. It has rec...

    W. C. Earnshaw, R. C. Allshire, B. E. Black, K. Bloom in Chromosome Research (2013)

  2. No Access

    Article

    Atomic structure of the ectodomain from HIV-1 gp41

    Fusion of viral and cellular membranes by the envelope glyco-protein gp120/gp41 effects entry of HIV-1 into the cell. The precursor, gp160, is cleaved post-translationally into gp120 and gp41 (refs 1,2), which...

    W. Weissenhorn, A. Dessen, S. C. Harrison, J. J. Skehel, D. C. Wiley in Nature (1997)

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    Article

    Crystal structure of the PI 3-kinase p85 amino-terminal SH2 domain and its phosphopeptide complexes

    Crystal structures of the amino-terminal SH2 domain of the p85α subunit of phosphatidylinositol (PI) 3-kinase, alone and in complex with phosphopeptides bearing pTyr-Met/Val-Xaa-Met motifs, show that phosphope...

    R.T. Nolte, M.J. Eck, J. Schlessinger, S.E. Shoelson in Nature Structural Biology (1996)

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    Article

    Structure of simian virus 40 at 3.8-Å resolution

    The crystallographically determined structure of simian virus 40 shows that the 72 pentamers of viral protein VP1, which form the outer shell, have identical conformations except for the C-terminal arms of the...

    R. C. Liddington, Y. Yan, J. Moulai, R. Sahli, T. L. Benjamin, S. C. Harrison in Nature (1991)

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    Article

    Structure of the represser–operator complex of bacteriophage 434

    The crystal structure of a specific complex between the DNA-binding domain of phage 434 represser and a synthetic 434 operator DNA shows interactions that determine sequence-dependent affinity. The represser ...

    J. E. Anderson, M. Ptashne, S. C. Harrison in Nature (1987)

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    Chapter

    A Bacteriophage Repressor/Operator Complex at 7 Å Resolution

    Possible mechanisms for sequence-specific affinity of proteins for DNA include: (1) ‘direct readout’ of base sequence by interactions of residues in the protein with functional groups on the DNA bases; (2) ‘in...

    S. C. Harrison, J. E. Anderson in Crystallography in Molecular Biology (1987)

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    Article

    Structure of the expanded state of tomato bushy stunt virus

    The full three-dimensional structure determination of tomato bushy stunt virus has shown how its protein subunit can accommodate to different packing environments in the viral coat and how the size of the part...

    I. K. Robinson, S. C. Harrison in Nature (1982)

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    Article

    Tomato bushy stunt virus at 2.9 Å resolution

    The polypeptide chain of a TBSV subunit folds into two domains, connected by a hinge, and a flexibly-linked N-terminal arm. Sixty of the 180 N-terminal arms inter-digitate in groups of three, in an unexpected ...

    S. C. Harrison, A. J. Olson, C. E. Schutt, F. K. Winkler, G. Bricogne in Nature (1978)

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    Article

    DNA arrangement in isometric phage heads

    DNA is wound tightly into phage heads in such a way that it tends to form layers concentric with the rigid protein shell. In P22 and wild-type lambda, DNA completely fills the internal volume, with a highly un...

    W. C. Earnshaw, S. C. Harrison in Nature (1977)

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    Article

    Tomato bushy stunt virus at 5.5-Å resolution

    The coat of tomato bushy stunt virus is built from protein subunits having rigid domains connected by a flexible hinge. Two states of the hinge are present in the T = 3 icosahedral structure. Each subunit has ...

    F. K. Winkler, C. E. Schutt, S. C. Harrison, G. Bricogne in Nature (1977)

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    Article

    Molecular Organization in the Sarcoplasmic Reticulum Membrane studied by X-ray Diffraction

    Orientated preparations of rabbit sarcoplasmic reticulum vesicles give X-ray diffraction maxima to a resolution of 16 Å. The calculated electron density profile shows that protein is distributed very asymmetri...

    Y. DUPONT, S. C. HARRISON, W. HASSELBACH in Nature (1973)