1t6f
From Proteopedia
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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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