1mnb
From Proteopedia
(New page: 200px<br /><applet load="1mnb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mnb" /> '''BIV TAT PEPTIDE (RESIDUES 68-81), NMR, MINIM...) |
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| - | [[Image:1mnb.gif|left|200px]]<br /><applet load="1mnb" size=" | + | [[Image:1mnb.gif|left|200px]]<br /><applet load="1mnb" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mnb" /> | caption="1mnb" /> | ||
'''BIV TAT PEPTIDE (RESIDUES 68-81), NMR, MINIMIZED AVERAGE STRUCTURE'''<br /> | '''BIV TAT PEPTIDE (RESIDUES 68-81), NMR, MINIMIZED AVERAGE STRUCTURE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The Tat protein of bovine immunodeficiency virus (BIV) binds to its target | + | The Tat protein of bovine immunodeficiency virus (BIV) binds to its target RNA, TAR, and activates transcription. A 14-amino acid arginine-rich peptide corresponding to the RNA-binding domain of BIV Tat binds specifically to BIV TAR, and biochemical and in vivo experiments have identified the amino acids and nucleotides required for binding. The solution structure of the RNA-peptide complex has now been determined by nuclear magnetic resonance spectroscopy. TAR forms a virtually continuous A-form helix with two unstacked bulged nucleotides. The peptide adopts a beta-turn conformation and sits in the major groove of the RNA. Specific contacts are apparent between critical amino acids in the peptide and bases and phosphates in the RNA. The structure is consistent with all biochemical data and demonstrates ways in which proteins can recognize the major groove of RNA. |
==About this Structure== | ==About this Structure== | ||
| - | 1MNB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1MNB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MNB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Blanchard, S.]] | [[Category: Blanchard, S.]] | ||
[[Category: Chen, L.]] | [[Category: Chen, L.]] | ||
| - | [[Category: Frankel, A | + | [[Category: Frankel, A D.]] |
| - | [[Category: Puglisi, J | + | [[Category: Puglisi, J D.]] |
[[Category: complex (regulatory protein/rna)]] | [[Category: complex (regulatory protein/rna)]] | ||
[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:56:55 2008'' |
Revision as of 11:56, 21 February 2008
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BIV TAT PEPTIDE (RESIDUES 68-81), NMR, MINIMIZED AVERAGE STRUCTURE
Overview
The Tat protein of bovine immunodeficiency virus (BIV) binds to its target RNA, TAR, and activates transcription. A 14-amino acid arginine-rich peptide corresponding to the RNA-binding domain of BIV Tat binds specifically to BIV TAR, and biochemical and in vivo experiments have identified the amino acids and nucleotides required for binding. The solution structure of the RNA-peptide complex has now been determined by nuclear magnetic resonance spectroscopy. TAR forms a virtually continuous A-form helix with two unstacked bulged nucleotides. The peptide adopts a beta-turn conformation and sits in the major groove of the RNA. Specific contacts are apparent between critical amino acids in the peptide and bases and phosphates in the RNA. The structure is consistent with all biochemical data and demonstrates ways in which proteins can recognize the major groove of RNA.
About this Structure
1MNB is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Solution structure of a bovine immunodeficiency virus Tat-TAR peptide-RNA complex., Puglisi JD, Chen L, Blanchard S, Frankel AD, Science. 1995 Nov 17;270(5239):1200-3. PMID:7502045
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