1MNB
BIV TAT PEPTIDE (RESIDUES 68-81), NMR, MINIMIZED AVERAGE STRUCTURE
1MNB の概要
| エントリーDOI | 10.2210/pdb1mnb/pdb |
| 分子名称 | BIV TAR RNA, BIV TAT PEPTIDE (2 entities in total) |
| 機能のキーワード | complex (regulatory protein-rna), transcription regulation, viral protein-rna complex, viral protein/rna |
| 細胞内の位置 | Host nucleus, host nucleolus: P19564 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 10653.39 |
| 構造登録者 | Puglisi, J.D.,Chen, L.,Blanchard, S.,Frankel, A.D. (登録日: 1996-07-25, 公開日: 1997-01-27, 最終更新日: 2024-05-22) |
| 主引用文献 | Puglisi, J.D.,Chen, L.,Blanchard, S.,Frankel, A.D. Solution structure of a bovine immunodeficiency virus Tat-TAR peptide-RNA complex. Science, 270:1200-1203, 1995 Cited by PubMed Abstract: 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. PubMed: 7502045主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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