1AJU

HIV-2 TAR-ARGININAMIDE COMPLEX, NMR, 20 STRUCTURES

1AJU の概要

• エントリーDOI: 10.2210/pdb1aju/pdb
• 関連するPDBエントリー: 1AKX
• 分子名称: TAR RNA, ARGININE (2 entities in total)
• 機能のキーワード: complex (ribonucleic acid-ligand), transcriptional activation, protein-rna interactions, rna
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9827.97

構造登録者

Brodsky, A.S.,Williamson, J.R. (登録日: 1997-05-10, 公開日: 1997-12-17, 最終更新日: 2024-05-22)

主引用文献

Brodsky, A.S.,Williamson, J.R.
Solution structure of the HIV-2 TAR-argininamide complex.
J.Mol.Biol., 267:624-639, 1997

PubMed Abstract: The trans-activating region (TAR) RNA-Tat protein interaction is important for activation of transciption in the human immunodeficiency virus (HIV). A model complex for this interaction composed of the two base bulge HIV-2 TAR and the amide derivative of arginine was studied by multidimensional heteronuclear NMR. Because of the improved spectral properties of the HIV-2 TAR complex, a larger number of NOEs in the bulge region were observed than in earlier studies of the HIV-1 TAR-argininamide complex. A total of 681 NOE distance restraints were collected and used to determine the solution structure of the HIV-2 TAR-argininamide complex. As observed in the previously proposed model from this lab, the two A-form stems co-axially stack and the critical U23 and the argininamide are located in the major groove. Model calculations including non-experimental restraints indicate that U23 is within hydrogen bonding distance to A27 consistent with the formation of a U x A x U base-triple. Base-triple formation helps open the major groove to increase the accessibility of G26 to hydrogen bond donors from the guanidinium group of argininamide. Argininamide binding is stabilized by stacking of the guanidinium group between the bases of A22 and U23, forming an argininamide sandwich.

PubMed: 9126842
DOI: 10.1006/jmbi.1996.0879

実験手法

SOLUTION NMR