User:Udayan Shevade/Sandbox1
From Proteopedia
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==== The Origin Binding Domain ==== | ==== The Origin Binding Domain ==== | ||
| - | The central obd monomer consists of five anti-parallel beta | + | The central obd monomer consists of <scene name='User:Udayan_Shevade/Sandbox1/Helix_and_sheet/1'>a five-strand anti-parallel beta sheet flanked by two pairs of alpha helices</scene>. These molecules arrange tightly into a hexameric left-handed spiral, with 6 obd's per turn. The conformation creates a central channel 60 Angstrom wide, large enough for dsDNA, and is highly positively charged <ref name="A"/>. Side-side interaction is crucial in hexamerization, for which residues <scene name='User:Udayan_Shevade/Sandbox1/Obd/2'>Phe 183 and Ser 185</scene> are crucial. Along the inner surface of the channel, residues implicated in DNA binding are <scene name='User:Udayan_Shevade/Sandbox1/Obd_153_154_155/3'>Asn 153, Arg 154, Thr 155 from the A motif</scene>; His 203, Arg 204 from the B2 motif; as well as His 201 and Arg 202. </StructureSection> |
Revision as of 17:00, 10 November 2011
SV40 Large T-Antigen
Introduction
The SV40 large T-antigen is a multifunctional regulatory protein encoded by Simian Virus 40, belonging to the AAA+ family of helicases [1]. It is responsible for initiation of replication, regulation of transcription and alteration of the host cell cycle to promote its infectivity.
Structure
T-antigen consists of an N-terminal J domain, a central origin-binding domain, and a C-terminal helicase domain [1].
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