1t6f

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(New page: 200px<br /> <applet load="1t6f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t6f, resolution 1.47&Aring;" /> '''Crystal Structure o...)
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[[Image:1t6f.gif|left|200px]]<br />
 
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<applet load="1t6f" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1t6f, resolution 1.47&Aring;" />
 
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'''Crystal Structure of the Coiled-coil Dimerization Motif of Geminin'''<br />
 
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==Overview==
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==Crystal Structure of the Coiled-coil Dimerization Motif of Geminin==
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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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<StructureSection load='1t6f' size='340' side='right'caption='[[1t6f]], [[Resolution|resolution]] 1.47&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1t6f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T6F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T6F FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.47&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t6f OCA], [https://pdbe.org/1t6f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t6f RCSB], [https://www.ebi.ac.uk/pdbsum/1t6f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t6f ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GEMI_HUMAN GEMI_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.<ref>PMID:9635433</ref> <ref>PMID:14993212</ref> <ref>PMID:22615398</ref> Inhibits the transcriptional activity of a subset of Hox proteins, enrolling them in cell proliferative control.<ref>PMID:9635433</ref> <ref>PMID:14993212</ref> <ref>PMID:22615398</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t6/1t6f_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1t6f ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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==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:15313623<ref>PMID:15313623</ref>
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1T6F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1T6F OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 1t6f" style="background-color:#fffaf0;"></div>
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[[Category: Auge, M.T.]]
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== References ==
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[[Category: Dumas, C.]]
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<references/>
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[[Category: Guichou, J.F.]]
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__TOC__
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[[Category: Maiorano, D.]]
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</StructureSection>
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[[Category: Mechali, M.]]
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[[Category: Homo sapiens]]
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[[Category: Padilla, A.]]
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[[Category: Large Structures]]
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[[Category: Thepaut, M.]]
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[[Category: Auge M-T]]
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[[Category: coiled-coil]]
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[[Category: Dumas C]]
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[[Category: Guichou J-F]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:21:26 2007''
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[[Category: Maiorano D]]
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[[Category: Mechali M]]
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[[Category: Padilla A]]
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[[Category: Thepaut M]]

Current revision

Crystal Structure of the Coiled-coil Dimerization Motif of Geminin

PDB ID 1t6f

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