1t6f

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==Overview==
==Overview==
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We have determined the crystal structure of the coiled-coil domain of, human geminin, a DNA synthesis inhibitor in higher eukaryotes. We show, that a peptide encompassing the five heptad repeats of the geminin leucine, zipper (LZ) domain is a dimeric parallel coiled coil characterized by a, unique pattern of internal polar residues and a negatively charged surface, that may target the basic domain of interacting partners. We show that the, LZ domain itself is not sufficient to inhibit DNA synthesis but upstream, and downstream residues are required. Analysis of a functional form of, geminin by density sedimentation indicates an oligomeric structure. X-ray, solution scattering experiments performed on a non-functional form of, geminin having upstream basic residues and the LZ domain show a tetramer, structure. Altogether, these results give a consistent identification and, mapping of geminin interacting regions onto structurally important, domains. They also suggest that oligomerization properties of geminin may, be implicated in its inhibitory activity of DNA synthesis.
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We have determined the crystal structure of the coiled-coil domain of human geminin, a DNA synthesis inhibitor in higher eukaryotes. We show that a peptide encompassing the five heptad repeats of the geminin leucine zipper (LZ) domain is a dimeric parallel coiled coil characterized by a unique pattern of internal polar residues and a negatively charged surface that may target the basic domain of interacting partners. We show that the LZ domain itself is not sufficient to inhibit DNA synthesis but upstream and downstream residues are required. Analysis of a functional form of geminin by density sedimentation indicates an oligomeric structure. X-ray solution scattering experiments performed on a non-functional form of geminin having upstream basic residues and the LZ domain show a tetramer structure. Altogether, these results give a consistent identification and mapping of geminin interacting regions onto structurally important domains. They also suggest that oligomerization properties of geminin may be implicated in its inhibitory activity of DNA synthesis.
==About this Structure==
==About this Structure==
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Crystal structure of the coiled-coil dimerization motif of geminin: structural and functional insights on DNA replication regulation., Thepaut M, Maiorano D, Guichou JF, Auge MT, Dumas C, Mechali M, Padilla A, J Mol Biol. 2004 Sep 3;342(1):275-87. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15313623 15313623]
Crystal structure of the coiled-coil dimerization motif of geminin: structural and functional insights on DNA replication regulation., Thepaut M, Maiorano D, Guichou JF, Auge MT, Dumas C, Mechali M, Padilla A, J Mol Biol. 2004 Sep 3;342(1):275-87. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15313623 15313623]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Auge, M.T.]]
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[[Category: Auge, M T.]]
[[Category: Dumas, C.]]
[[Category: Dumas, C.]]
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[[Category: Guichou, J.F.]]
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[[Category: Guichou, J F.]]
[[Category: Maiorano, D.]]
[[Category: Maiorano, D.]]
[[Category: Mechali, M.]]
[[Category: Mechali, M.]]
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[[Category: coiled-coil]]
[[Category: coiled-coil]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:55:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:10:21 2008''

Revision as of 13:10, 21 February 2008


1t6f, resolution 1.47Å

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Crystal Structure of the Coiled-coil Dimerization Motif of Geminin

Overview

We have determined the crystal structure of the coiled-coil domain of human geminin, a DNA synthesis inhibitor in higher eukaryotes. We show that a peptide encompassing the five heptad repeats of the geminin leucine zipper (LZ) domain is a dimeric parallel coiled coil characterized by a unique pattern of internal polar residues and a negatively charged surface that may target the basic domain of interacting partners. We show that the LZ domain itself is not sufficient to inhibit DNA synthesis but upstream and downstream residues are required. Analysis of a functional form of geminin by density sedimentation indicates an oligomeric structure. X-ray solution scattering experiments performed on a non-functional form of geminin having upstream basic residues and the LZ domain show a tetramer structure. Altogether, these results give a consistent identification and mapping of geminin interacting regions onto structurally important domains. They also suggest that oligomerization properties of geminin may be implicated in its inhibitory activity of DNA synthesis.

About this Structure

1T6F is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

Reference

Crystal structure of the coiled-coil dimerization motif of geminin: structural and functional insights on DNA replication regulation., Thepaut M, Maiorano D, Guichou JF, Auge MT, Dumas C, Mechali M, Padilla A, J Mol Biol. 2004 Sep 3;342(1):275-87. PMID:15313623

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