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1wlq

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(New page: 200px<br /><applet load="1wlq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wlq, resolution 2.80&Aring;" /> '''Strucure of Geminin-...)
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[[Image:1wlq.gif|left|200px]]<br /><applet load="1wlq" size="450" color="white" frame="true" align="right" spinBox="true"
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#REDIRECT [[2zxx]] This PDB entry is obsolete and replaced by 2zxx
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caption="1wlq, resolution 2.80&Aring;" />
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'''Strucure of Geminin-Cdt1 complex'''<br />
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==Overview==
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To maintain chromosome stability in eukaryotic cells, replication origins, must be licensed by loading mini-chromosome maintenance (MCM2-7) complexes, once and only once per cell cycle. This licensing control is achieved, through the activities of geminin and cyclin-dependent kinases. Geminin, binds tightly to Cdt1, an essential component of the replication licensing, system, and prevents the inappropriate reinitiation of replication on an, already fired origin. The inhibitory effect of geminin is thought to, prevent the interaction between Cdt1 and the MCM helicase. Here we, describe the crystal structure of the mouse geminin-Cdt1 complex using, tGeminin (residues 79-157, truncated geminin) and tCdt1 (residues 172-368, truncated Cdt1). The amino-terminal region of a coiled-coil dimer of, tGeminin interacts with both N-terminal and carboxy-terminal parts of, tCdt1. The primary interface relies on the steric complementarity between, the tGeminin dimer and the hydrophobic face of the two short N-terminal, helices of tCdt1 and, in particular, Pro 181, Ala 182, Tyr 183, Phe 186, and Leu 189. The crystal structure, in conjunction with our biochemical, data, indicates that the N-terminal region of tGeminin might be required, to anchor tCdt1, and the C-terminal region of tGeminin prevents access of, the MCM complex to tCdt1 through steric hindrance.
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==About this Structure==
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1WLQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WLQ OCA].
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==Reference==
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Structural basis for inhibition of the replication licensing factor Cdt1 by geminin., Lee C, Hong B, Choi JM, Kim Y, Watanabe S, Ishimi Y, Enomoto T, Tada S, Kim Y, Cho Y, Nature. 2004 Aug 19;430(7002):913-7. Epub 2004 Aug 1. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15286659 15286659]
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[[Category: Mus musculus]]
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[[Category: Protein complex]]
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[[Category: Cho, Y.]]
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[[Category: Choi, J.M.]]
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[[Category: Enomoto, T.]]
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[[Category: Hong, B.]]
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[[Category: Ishimi, Y.]]
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[[Category: Kim, Y.]]
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[[Category: Lee, C.]]
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[[Category: Tada, S.]]
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[[Category: Watanabe, S.]]
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[[Category: coiled-coil]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:30:59 2007''
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Current revision

  1. REDIRECT 2zxx This PDB entry is obsolete and replaced by 2zxx

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