User:Guilherme Gonzalez/Sandbox 1

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Function

HSH155^{HEAT is a core splicing factor that is associated with the U2 small nuclear ribonucleoproteins complex (U2 snRNA), a component of the spliceosome of Saccharomyces cerevisiae. The HSH155 is a major component to the splicing of the pre-mRNA, this protein binds with the pre-mRNA upstream of the intron branching site no matter the sequence of this RNA, anchoring the U2 snRNA to the pre-mRNA.}

The HSH155 is composed by a single peptide, the structure of the region closer to the N-terminal is still unresolved but the rest of this protein is composed by a series of alpha helices in tandem, denominated HEAT repeat, this structure is characterized by repetitions of two alpha helices linked by a short loop, forming a solenoid form that resembles the letter “C”.

This structure is essential to the function of this protein, allowing ligants to interact with the innermost part of this molecule and alter its opening, being capable of small regulations in its capacity to interact with the pre-RNAm and other molecules of the U2 snRNA. Besides that, this structure has two main states: Open and Closed. This can be regulated and permits the interaction and the fixation of the pre-RNAm, and this process allows the formation of the A complex during the splicing.

In the box at the right, it is possible to see its in a space-fill model obtained by electron microscopy at 9 Å resolution. However, to cover some important aspects of the structure and function of the molecule, it is particularly useful to represent its . This previous representation shows that the alpha helices are a major component of this protein, in you can also see that, now with red to represent alpha helices and blue for the loops.

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.