1uii

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{{STRUCTURE_1uii| PDB=1uii | SCENE= }}
{{STRUCTURE_1uii| PDB=1uii | SCENE= }}
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'''Crystal structure of Geminin coiled-coil domain'''
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===Crystal structure of Geminin coiled-coil domain===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15260975 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15260975}}
==About this Structure==
==About this Structure==
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[[Category: Geminin]]
[[Category: Geminin]]
[[Category: Human]]
[[Category: Human]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:16:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:58:50 2008''

Revision as of 09:58, 28 July 2008

Image:1uii.png

Template:STRUCTURE 1uii

Crystal structure of Geminin coiled-coil domain

Template:ABSTRACT PUBMED 15260975

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

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