Molecular Dynamics and Thermodynamics of Protein−RNA Interactions: Mutation of a Conserved Aromatic Residue Modifies Stacking Interactions and Structural Adaptation in the U1A−Stem Loop 2 RNA Complex-Reference-Cited by-同舟云学术

Molecular Dynamics and Thermodynamics of Protein−RNA Interactions: Mutation of a Conserved Aromatic Residue Modifies Stacking Interactions and Structural Adaptation in the U1A−Stem Loop 2 RNA Complex

Published:2001-02-20 Issue:11 Volume:123 Page:2548-2551
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Blakaj Dukagjin M.¹,McConnell Kevin J.¹,Beveridge David L.¹,Baranger Anne M.¹

Affiliation:

1. Contribution from the Chemistry Department and Molecular Biophysics Program, Wesleyan University, Middletown, Connecticut 06459

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja005538j

Reference38 articles.

1. RNA RECOGNITION BY RNP PROTEINS DURING RNA PROCESSING

2. RNA binding mediates the local cooperativity between the β-sheet and the C-terminal tail of the human U1A RBD1 protein

3. RNA recognition by the human U1A protein is mediated by a network of local cooperative interactions that create the optimal binding surface

4. Recognition of an Essential Adenine at a Protein−RNA Interface: Comparison of the Contributions of Hydrogen Bonds and a Stacking Interaction

5. Crystal structure at 1.92 Å resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin

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