From Proteopedia

Introduction

Hrp1 is a polyadenylation factor found in Saccharomyces cervisiae (yeast).

Relationships to other proteins

Structure

Hrp1 is composed of two RNP-type RNA-binding domains (RBDs) arranged in tandem.

Figure 1: Cartoon representation of the Hrp1-PEE complex. The RNA is shown as a stick model and is colored by element. Notice the interface between the ß-sheets of Hrp1 and the RNA.

Crucial Interactions

The interface between Hrp1 and its target RNA sequence is dominated by interactions between key aromatic residues and RNA bases. Hydrophilic residues of Hrp1 provide base specificity through hydrogen bonding. Most of the key residues that interact with the RNA can be found in the ß-sheet region of Hrp1; however, loops and the interdomain linker are also essential for Hrp1-RNA recognition.

Relevance

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

References

1. Pérez-Cañadillas, J. Grabbing The Message: Structural Basis Of Mrna 3′UTR Recognition By Hrp1. The EMBO Journal 2006, 25, 3167-3178. 2. Cléry, A.; Blatter, M.; Allain, F. RNA Recognition Motifs: Boring? Not Quite. Current Opinion in Structural Biology 2008, 18, 290-298. 3. Guo, Z.; Sherman, F. 3′-End-Forming Signals Of Yeast Mrna. Trends in Biochemical Sciences 1996, 21, 477-481. 4. Kessler, M.; Henry, M.; Shen, E.; Zhao, J.; Gross, S.; Silver, P.; Moore, C. Hrp1, A Sequence-Specific RNA-Binding Protein That Shuttles Between The Nucleus And The Cytoplasm, Is Required For Mrna 3'-End Formation In Yeast. Genes & Development 1997, 11, 2545-2556. 5. Leeper, T.; Qu, X.; Lu, C.; Moore, C.; Varani, G. Novel Protein–Protein Contacts Facilitate Mrna 3′-Processing Signal Recognition By Rna15 And Hrp1. Journal of Molecular Biology 2010, 401, 334-349. 6. The PyMol Molecular Graphics System, Version 2.0 Schrödinger, LLC. (for structural depictions)