User:Savannah Davis/Sandbox 1
From Proteopedia
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| - | + | =Introduction= | |
| - | + | <Structure load='2cjk' size='350' frame='true' align='right' caption='Hrp1' scene='Insert optional scene name here' /> | |
| - | + | Hrp1 is a polyadenylation factor found in Saccharomyces cervisiae (yeast). | |
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| - | == | + | ==Relationships to other proteins== |
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| - | == | + | =Structure= |
| + | Hrp1 is composed of two RNP-type RNA-binding domains (RBDs) arranged in tandem with a typical ßαßßαß architecture. The two RBDs have similar topolgies, both containing a central antiparallel four-stranded <scene name='78/781960/Beta_sheet/1'>ß-sheet</scene> with two α-helices running across one face. | ||
| + | [[Image:Hrp1 structure cropped for protopedia.png|350 px|left|thumb|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.]] | ||
| + | ==Hrp1-RNA interactions== | ||
| + | The <scene name='78/781960/Hrp1-rna_interface_surface/2'>interface</scene> between Hrp1 and its target RNA sequence is dominated by interactions between key aromatic residues and RNA bases. Only six RNA bases, (AU)3, form specific contacts with Hrp1. 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. Perhaps the most important Hrp1-RNA interaction is the <scene name='78/781960/Hrp1_scene_ade4trp168/2'>interaction between Ade4 and Trp168</scene> (a conserved residue). In this case, Trp168 stacks on Ade4 and forms crucial base-specific hydrogen bonds. | ||
| - | == Hrp1 == | ||
| - | + | <scene name='78/781945/Interaction_between_domains/5'>Interaction between RRM domains</scene> | |
| - | </ | + | <scene name='78/781945/Linker_rna/1'>Interaction between linker and RNA</scene> |
| - | == | + | |
| + | <scene name='78/781952/Ua_repeats/2'>(AU)3</scene> | ||
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| + | =Relevance= | ||
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| + | =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) | ||
<references/> | <references/> | ||
Current revision
Contents |
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 with a typical ßαßßαß architecture. The two RBDs have similar topolgies, both containing a central antiparallel four-stranded with two α-helices running across one face.
Hrp1-RNA interactions
The between Hrp1 and its target RNA sequence is dominated by interactions between key aromatic residues and RNA bases. Only six RNA bases, (AU)3, form specific contacts with Hrp1. 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. Perhaps the most important Hrp1-RNA interaction is the (a conserved residue). In this case, Trp168 stacks on Ade4 and forms crucial base-specific hydrogen bonds.
Relevance
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)
