1z1d
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1z1d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z1d" /> '''Structural Model for the interaction betwee...)
Next diff →
Revision as of 18:21, 12 November 2007
|
Structural Model for the interaction between RPA32 C-terminal domain and SV40 T antigen origin binding domain.
Overview
Simian virus 40 (SV40) provides a model system for the study of eukaryotic, DNA replication, in which the viral protein, large T antigen (Tag), marshals human proteins to replicate the viral minichromosome. SV40, replication requires interaction of Tag with the host single-stranded, DNA-binding protein, replication protein A (hRPA). The C-terminal domain, of the hRPA32 subunit (RPA32C) facilitates initiation of replication, but, whether it interacts with Tag is not known. Affinity chromatography and, NMR revealed physical interaction between hRPA32C and the Tag origin, DNA-binding domain, and a structural model of the complex was determined., Point mutations were then designed to reverse charges in the binding, sites, resulting in substantially reduced binding affinity. Corresponding, mutations introduced into intact hRPA impaired initiation of replication, and primosome activity, implying that this interaction has a critical role, in assembly and progression of the SV40 replisome.
About this Structure
1Z1D is a Protein complex structure of sequences from Homo sapiens and Simian virus 40. Full crystallographic information is available from OCA.
Reference
Insights into hRPA32 C-terminal domain--mediated assembly of the simian virus 40 replisome., Arunkumar AI, Klimovich V, Jiang X, Ott RD, Mizoue L, Fanning E, Chazin WJ, Nat Struct Mol Biol. 2005 Apr;12(4):332-9. Epub 2005 Mar 27. PMID:15793585
Page seeded by OCA on Mon Nov 12 20:28:18 2007
