1tvt

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(New page: 200px<br /><applet load="1tvt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tvt" /> '''STRUCTURE OF THE EQUINE INFECTIOUS ANEMIA VI...)
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'''STRUCTURE OF THE EQUINE INFECTIOUS ANEMIA VIRUS TAT PROTEIN'''<br />
'''STRUCTURE OF THE EQUINE INFECTIOUS ANEMIA VIRUS TAT PROTEIN'''<br />
==Overview==
==Overview==
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Trans-activator (Tat) proteins regulate the transcription of lentiviral, DNA in the host cell genome. These RNA binding proteins participate in the, life cycle of all known lentiviruses, such as the human immunodeficiency, viruses (HIV) or the equine infectious anemia virus (EIAV). The consensus, RNA binding motifs [the trans-activation responsive element (TAR)] of, HIV-1 as well as EIAV Tat proteins are well characterized. The structure, of the 75-amino acid EIAV Tat protein in solution was determined by two-, and three-dimensional nuclear magnetic resonance methods and molecular, dynamics calculations. The protein structure exhibits a well-defined, hydrophobic core of 15 amino acids that serves as a scaffold for two, flexible domains corresponding to the NH2- and COOH-terminal regions. The, core region is a strictly conserved sequence region among the known Tat, proteins. The structural data can be used to explain several of the, observed features of Tat proteins.
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Trans-activator (Tat) proteins regulate the transcription of lentiviral DNA in the host cell genome. These RNA binding proteins participate in the life cycle of all known lentiviruses, such as the human immunodeficiency viruses (HIV) or the equine infectious anemia virus (EIAV). The consensus RNA binding motifs [the trans-activation responsive element (TAR)] of HIV-1 as well as EIAV Tat proteins are well characterized. The structure of the 75-amino acid EIAV Tat protein in solution was determined by two- and three-dimensional nuclear magnetic resonance methods and molecular dynamics calculations. The protein structure exhibits a well-defined hydrophobic core of 15 amino acids that serves as a scaffold for two flexible domains corresponding to the NH2- and COOH-terminal regions. The core region is a strictly conserved sequence region among the known Tat proteins. The structural data can be used to explain several of the observed features of Tat proteins.
==About this Structure==
==About this Structure==
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1TVT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equine_infectious_anemia_virus Equine infectious anemia virus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TVT OCA].
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1TVT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equine_infectious_anemia_virus Equine infectious anemia virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TVT OCA].
==Reference==
==Reference==
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[[Category: transcription regulation]]
[[Category: transcription regulation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:49:56 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:17:55 2008''

Revision as of 13:17, 21 February 2008


1tvt

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STRUCTURE OF THE EQUINE INFECTIOUS ANEMIA VIRUS TAT PROTEIN

Overview

Trans-activator (Tat) proteins regulate the transcription of lentiviral DNA in the host cell genome. These RNA binding proteins participate in the life cycle of all known lentiviruses, such as the human immunodeficiency viruses (HIV) or the equine infectious anemia virus (EIAV). The consensus RNA binding motifs [the trans-activation responsive element (TAR)] of HIV-1 as well as EIAV Tat proteins are well characterized. The structure of the 75-amino acid EIAV Tat protein in solution was determined by two- and three-dimensional nuclear magnetic resonance methods and molecular dynamics calculations. The protein structure exhibits a well-defined hydrophobic core of 15 amino acids that serves as a scaffold for two flexible domains corresponding to the NH2- and COOH-terminal regions. The core region is a strictly conserved sequence region among the known Tat proteins. The structural data can be used to explain several of the observed features of Tat proteins.

About this Structure

1TVT is a Single protein structure of sequence from Equine infectious anemia virus. Full crystallographic information is available from OCA.

Reference

Structure of the equine infectious anemia virus Tat protein., Willbold D, Rosin-Arbesfeld R, Sticht H, Frank R, Rosch P, Science. 1994 Jun 10;264(5165):1584-7. PMID:7515512

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