User:Udayan Shevade/Sandbox1
From Proteopedia
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===== The Origin Binding Domain ===== | ===== The Origin Binding Domain ===== | ||
| - | + | {{STRUCTURE_1tbd| PDB=1tbd | SCENE= }} | |
The central obd monomer consists of five anti-parallel beta sheets flanked on both sides by pairs of alpha helices. 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 both hydrophobic and 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/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 <ref name="A"/>. | The central obd monomer consists of five anti-parallel beta sheets flanked on both sides by pairs of alpha helices. 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 both hydrophobic and 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/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 <ref name="A"/>. | ||
Revision as of 00:46, 9 November 2011
Contents |
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].
The Origin Binding Domain
The central obd monomer consists of five anti-parallel beta sheets flanked on both sides by pairs of alpha helices. 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 both hydrophobic and highly positively charged [1]. Side-side interaction is crucial in hexamerization, for which residues are crucial. Along the inner surface of the channel, residues implicated in DNA binding are ; His 203, Arg 204 from the B2 motif; as well as His 201 and Arg 202 [1].
