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PMID: 11463612 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Molecular dynamics simulation of the human U2B" protein complex with U2 snRNA hairpin IV in aqueous solution.

Biophysical journal ·Vol. 81 ·No. 2 ·2001-08-00 ·Pages 630-42

Guo JX, Gmeiner WH

Abstract

A 2200-ps molecular dynamics (MD) simulation of the U2 snRNA hairpin IV/U2B" complex was performed in aqueous solution using the particle mesh Ewald method to consider long-range electrostatic interactions. To investigate the interaction and recognition process between the RNA and protein, the free energy contributions resulting from individual amino acids of the protein component of the RNA/protein complex were calculated using the recently developed glycine-scanning method. The results revealed that the loop region of the U2 snRNA hairpin IV interacted mainly with three regions of the U2B" protein: 1) beta 1-helix A, 2) beta 2-beta 3, and 3) beta 4-helix C. U2 snRNA hairpin IV bound U2B" in a similar orientation as that previously described for U1 snRNA with the U1A' protein; however, the details of the interaction differed in several aspects. In particular, beta 1-helix A and beta 4-helix C in U2B" were not observed to interact with RNA in the U1A' protein complex. Most of the polar and charged residues in the interacting regions had larger mutant free energies than the nonpolar residues, indicating that electrostatic interactions were important for stabilizing the RNA/protein complex. The interaction was further stabilized by a network of hydrogen bonds and salt bridges formed between RNA and protein that was maintained throughout the MD trajectory. In addition to the direct interactions between RNA and the protein, solvent-mediated interactions also contributed significantly to complex stability. A detailed analysis of the ordered water molecules in the hydration of the RNA/protein complex revealed that bridged water molecules reside at the interface of RNA and protein as long as 2100 ps in the 2200-ps trajectory. At least 20 bridged water molecules, on average, contributed to the instantaneous stability of the RNA/protein complex. The stabilizing interaction energy due to bridging water molecules was obtained from ab initio Hartree-Fock and density functional theory calculations.

MeSH Terms
Autoantigens Base Sequence Binding Sites Computer Simulation Glycine/genetics,metabolism Humans Hydrogen Bonding Models, Molecular Molecular Conformation Mutagenesis Protein Binding RNA, Small Nuclear/chemistry,genetics,metabolism RNA-Binding Proteins/chemistry,genetics,metabolism Ribonucleoprotein, U1 Small Nuclear/chemistry Ribonucleoprotein, U2 Small Nuclear/chemistry,genetics,metabolism Ribonucleoproteins, Small Nuclear Solutions/chemistry Static Electricity Thermodynamics Water/chemistry,metabolism snRNP Core Proteins
Chemicals
Autoantigens RNA, Small Nuclear RNA-Binding Proteins Ribonucleoprotein, U1 Small Nuclear Ribonucleoprotein, U2 Small Nuclear Ribonucleoproteins, Small Nuclear SNRPB2 protein, human Solutions U1 small nuclear RNA U1A protein U2 small nuclear RNA snRNP Core Proteins Water Glycine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Guo J X
Eppley Institute, University of Nebraska Medical Center, Omaha, Nebraska, 68198-6805 USA.
Gmeiner W H
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Article Info
Journal
Biophysical journal
Abbr.
Biophys J
ISSN
0006-3495
Published
2001-08-00
Pages
630-42
Language
English
Region
United States
NLM ID
0370626
PMCID
PMC1301540
Subset
IM
Grants
NCPDCID CDC HHS · NCI 36727 · United States
NCPDCID CDC HHS · NCI 60612 · United States
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