ORGN 696 |
| Ying Zhao1, David Kombo2, K. Suzie Byun1, David L. Beveridge3, and Anne M. Baranger1. (1) Department of Chemistry, Wesleyan University, Middletown, CT 06459, (2) BioNumerik Pharmaceuticals, Inc, 8122 Datapoint Drive, San Antonio, TX 78229, (3) Department of Chemistry and Molecular Biophysics Program, Wesleyan University, Lawn Avenue, Middletown, CT 06459 |
| The RNA recognition motif (RRM) is one of the largest families of RNA binding domains. In the complex formed between the N-terminal RRM of the U1A protein and stem loop 2 of U1 snRNA, A6 and C7 of RNA are stacked with a highly conserved aromatic amino acid, Phe56. Substitution of Phe56 with Ala resulted in a large destabilization of the complex. We have designed two modified adenosines, in which a phenyl group is linked to the adenosine such that it may replace the phenyl group that is eliminated by the Phe56Ala mutation in the complex. Incorporation of these modified adenosines into stem loop 2 RNA stabilizes the complex formed with Phe56Ala. However, it is unclear how the modified base contributes to this stabilization. Molecular dynamics simulations were carried out to investigate the interactions that contribute to the stabilization of the complex formed between Phe56Ala U1A protein and A6-4CPh RNA. |
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Proteins, Peptides, Amino Acids, and Nucleotides
8:30 AM-11:30 AM, Thursday, September 11, 2003 Sheraton New York -- Royal Ballroom B, Oral
Division of Organic Chemistry |