BIOL 43 |
| The RNA recognition motif (RRM) is one of the most common motifs found in RNA binding proteins. RRM-containing proteins are involved in transport and storage of RNA and play crucial roles in regulating gene expression. The U1A protein is a good model system for investigating RRM-RNA recognition due its high affinity and specificity to stem loop 2 of U1 snRNA. The U1A protein is part of the U1 small nuclear ribonucleoprotein particle, which is involved in RNA Structures of the free and bound wild type U1A, determined by NMR and X-ray crystallography have been reported. Previously we showed that mutation of a highly conserved phenylalanine in RNP1 to alanine (F56A) results in a loss in stability of the complex of about 5 kcal/mol. We are using NMR methods to investigate the structure of U1A proteins (wild type and F56A mutant) in the free and bound state in order to identify the possible causes of the binding energy loss upon mutation. Ongoing NMR studies that focus on solving the NMR structure of the F56A mutant in the free and bound state will be presented. |
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Protein Structure and Folding
4:30 PM-6:30 PM, Sunday, 10 September 2006 Moscone Center -- Hall D, Poster
Sci-Mix
Division of Biological Chemistry |