User:Udayan Shevade/Sandbox1
From Proteopedia
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=== Introduction === | === Introduction === | ||
- | The '''large tumor antigen''' is a multifunctional regulatory protein encoded by Simian Virus 40. It is classified under the AAA+ family of helicases <ref name="A">PMID:8946857</ref>. Noteworthy for its versatility, the protein is responsible for initiation of viral DNA replication, regulation of viral transcription and transformation of the host cell to promote viral infectivity. Large T-antigen is an early gene product of SV40 and is produced via differential mRNA splicing. | + | The '''SV40 large tumor antigen''' is a multifunctional regulatory protein encoded by Simian Virus 40. It is classified under the AAA+ family of helicases <ref name="A">PMID:8946857</ref>. Noteworthy for its versatility, the protein is responsible for initiation of viral DNA replication, regulation of viral transcription and transformation of the host cell to promote viral infectivity. Large T-antigen is an early gene product of SV40 and is produced via differential mRNA splicing. |
Revision as of 21:48, 12 November 2011
Contents |
SV40 Large T Antigen
Introduction
The SV40 large tumor antigen is a multifunctional regulatory protein encoded by Simian Virus 40. It is classified under the AAA+ family of helicases [1]. Noteworthy for its versatility, the protein is responsible for initiation of viral DNA replication, regulation of viral transcription and transformation of the host cell to promote viral infectivity. Large T-antigen is an early gene product of SV40 and is produced via differential mRNA splicing.
Structure
T antigen is a 708-amino acid protein with three major domains: an N-terminal J domain, a central origin-binding domain, and a C-terminal helicase domain [2]. The activities of each are covered briefly below.
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1svm, resolution 1.94Å () | |||||||||
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Ligands: | , , | ||||||||
Related: | 1svl, 1svo | ||||||||
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Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
Coordinates: | save as pdb, mmCIF, xml |
Helicase
The monomer of the hexameric helicase contains a AAA+ domain. Each monomer binds and hydrolyzes an ATP in the presence of magnesium ion and drives an overall conformational change in the hexamer.