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| | {{STRUCTURE_1arj| PDB=1arj | SCENE= }} | | {{STRUCTURE_1arj| PDB=1arj | SCENE= }} |
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| - | '''ARG-BOUND TAR RNA, NMR'''
| + | ===ARG-BOUND TAR RNA, NMR=== |
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| - | ==Overview==
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| - | The human immunodeficiency virus type-1 (HIV-1) Tat protein stimulates transcriptional elongation. Tat is introduced to the transcription machinery by binding to the transactivation response region (TAR) RNA stem-loop encoded by the 5' leader sequence found on all HIV-1 mRNAs. We have used multidimensional heteronuclear NMR to determine the structure of the TAR RNA in the presence of the ADP-1 polypeptide, a 37-mer that carries the minimal RNA recognition region of the Tat protein and closely mimics Tat binding specificity. In the presence of a variety of ligands, including ADP-1, related basic peptides and the amino acid derivative argininamide, the bulge region of TAR undergoes a local conformational rearrangement and forms a more stable structure. The structure of TAR in the bound form has been determined from over 1000 NMR-derived constraints. The U23 residue at the 5' end of the bulge is positioned near G26 and A27 in the major groove, rather than stacked on A22 as in the free TAR. U23 and G26 are brought into close proximity by contacts to the guanidinium group and side-chain amide group of a common arginine residue. However, the interaction of this guanidinium group with TAR is not the only source of binding specificity. Besides NOEs to the arginine residue participating in the conformational change, ADP-1 shows additional intermolecular NOEs to TAR, suggesting that there are multiple points of contacts between TAR RNA and residues from the basic and core regions of Tat. These structural results provide important clues towards the identification of small molecular mass and/or peptidomimetic inhibitors of the essential Tat-TAR interaction. | + | The line below this paragraph, {{ABSTRACT_PUBMED_7563092}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 7563092 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_7563092}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ARJ OCA]. | + | Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ARJ OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Nmr peptide-bound structure]] | | [[Category: Nmr peptide-bound structure]] |
| | [[Category: Nucleic acid]] | | [[Category: Nucleic acid]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:37:20 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:28:20 2008'' |
Revision as of 14:28, 30 June 2008
Template:STRUCTURE 1arj
ARG-BOUND TAR RNA, NMR
Template:ABSTRACT PUBMED 7563092
About this Structure
Full experimental information is available from OCA.
Reference
The structure of the human immunodeficiency virus type-1 TAR RNA reveals principles of RNA recognition by Tat protein., Aboul-ela F, Karn J, Varani G, J Mol Biol. 1995 Oct 20;253(2):313-32. PMID:7563092
Page seeded by OCA on Mon Jun 30 17:28:20 2008
