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Revision as of 23:51, 2 April 2018

Contents 1 HRP1 1.1 RNA Binding 1.1.1 Adenines 1.2 Disease 1.3 Relevance 1.4 Structural highlights 1.5 References

HRP1

HRP1 is found in Saccharomyces cerevisiae, commonly known as "baker's yeast." It was discovered via solution NMR and then released to the RCSB Protein Data Bank with the ID "2CJK" in 2006. HRP1 is the RNA recognition domain of the Cleavage Factor Complex, positioning the RNA cleavage site prior to polyadenylation. It is composed of 2 RNA binding domains that recognize a specific 5'-AUAUAU-3' sequence of RNA.

spinqualitylabelsall models 2CJK Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

This is a default text for your page Evie Nguyen/Sandbox 1. Click above on edit this page to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia ^[1] or to the article describing Jmol ^[2] to the rescue.

RNA Binding

The ribonucleotides of the recognized sequence 5'-AUAUAU-3' are designated from 5'-3' Ade2, Ade4, and Ade6; and Ura3, Ura5, and Ura7. The first two bases, Ade2 and Ura3, bind to the second RNA binding domain, and the remaining bases of the sequence bind to the first RNA binding domain. Each ribonucleotide has distinguishing interactions with the protein including

Adenines

Disease

Relevance

Structural highlights

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.

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References

1. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644