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Brief Communication
Nature Structural & Molecular Biology  11, 1021 - 1022 (2004)
Published online: 19 September 2004; | doi:10.1038/nsmb835

Molecular structure of human geminin

Andrei L Okorokov1, 3, 4, 5, Elena V Orlova2, 5, Sarah R Kingsbury3, Claire Bagneris1, Ulrich Gohlke1, Gareth H Williams3, 4 & Kai Stoeber3, 4

1  Bloomsbury Centre of Structural Biology, Birkbeck College, Malet Street, London, WC1E 7HX, UK.

2  School of Crystallography, Birkbeck College, Malet Street, London, WC1E 7HX, UK.

3  Wolfson Institute for Biomedical Research, University College London, Gower Street, London, WC1E 6BT, UK.

4  Department of Histopathology, Royal Free and University College Medical School, University College London, London, WC1E 6JJ, UK.

5  These authors contributed equally to this work.

Correspondence should be addressed to Gareth H Williams gareth.williams@ucl.ac.uk
The origin licensing repressor geminin is a unique bifunctional protein providing a molecular link between cellular proliferation, differentiation and genomic stability. Here we report the first molecular structure of human geminin, determined by EM and image processing at a resolution of 17.5 Å. The geminin molecule is a tetramer formed by two dimers with monomers interacting via coiled-coil domains. The unusual structural organization of geminin provides molecular insight into its bifunctional nature.


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Nature Structural & Molecular Biology
ISSN: 1545-9993
EISSN: 1545-9985
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