1uii
From Proteopedia
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| - | [[Image:1uii.jpg|left|200px]] | + | [[Image:1uii.jpg|left|200px]] |
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| - | '''Crystal structure of Geminin coiled-coil domain''' | + | {{Structure |
| + | |PDB= 1uii |SIZE=350|CAPTION= <scene name='initialview01'>1uii</scene>, resolution 2.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= GMNN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of Geminin coiled-coil domain''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1UII is a [ | + | 1UII is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UII OCA]. |
==Reference== | ==Reference== | ||
| - | A dimerized coiled-coil domain and an adjoining part of geminin interact with two sites on Cdt1 for replication inhibition., Saxena S, Yuan P, Dhar SK, Senga T, Takeda D, Robinson H, Kornbluth S, Swaminathan K, Dutta A, Mol Cell. 2004 Jul 23;15(2):245-58. PMID:[http:// | + | A dimerized coiled-coil domain and an adjoining part of geminin interact with two sites on Cdt1 for replication inhibition., Saxena S, Yuan P, Dhar SK, Senga T, Takeda D, Robinson H, Kornbluth S, Swaminathan K, Dutta A, Mol Cell. 2004 Jul 23;15(2):245-58. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15260975 15260975] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: human]] | [[Category: human]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:32:26 2008'' |
Revision as of 12:32, 20 March 2008
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| , resolution 2.00Å | |||||||
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| Gene: | GMNN (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Geminin coiled-coil domain
Overview
Geminin is a cellular protein that associates with Cdt1 and inhibits Mcm2-7 loading during S phase. It prevents multiple cycles of replication per cell cycle and prevents episome replication. It also directly inhibits the HoxA11 transcription factor. Here we report that geminin forms a parallel coiled-coil homodimer with atypical residues in the dimer interface. Point mutations that disrupt the dimerization abolish interaction with Cdt1 and inhibition of replication. An array of glutamic acid residues on the coiled-coil domain surface interacts with positive charges in the middle of Cdt1. An adjoining region interacts independently with the N-terminal 100 residues of Cdt1. Both interactions are essential for replication inhibition. The negative residues on the coiled-coil domain and a different part of geminin are also required for interaction with HoxA11. Therefore a rigid cylinder with negative surface charges is a critical component of a bipartite interaction interface between geminin and its cellular targets.
About this Structure
1UII is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
A dimerized coiled-coil domain and an adjoining part of geminin interact with two sites on Cdt1 for replication inhibition., Saxena S, Yuan P, Dhar SK, Senga T, Takeda D, Robinson H, Kornbluth S, Swaminathan K, Dutta A, Mol Cell. 2004 Jul 23;15(2):245-58. PMID:15260975
Page seeded by OCA on Thu Mar 20 14:32:26 2008
