1t6f
Crystal Structure of the Coiled-coil Dimerization Motif of Geminin
Structural highlights
FunctionGEMI_HUMAN Inhibits DNA replication by preventing the incorporation of MCM complex into pre-replication complex (pre-RC). It is degraded during the mitotic phase of the cell cycle. Its destruction at the metaphase-anaphase transition permits replication in the succeeding cell cycle.[1] [2] [3] Inhibits the transcriptional activity of a subset of Hox proteins, enrolling them in cell proliferative control.[4] [5] [6] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe 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. 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[7] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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